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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 莊榮輝 | |
| dc.contributor.author | Guang-Huar Young | en |
| dc.contributor.author | 楊光華 | zh_TW |
| dc.date.accessioned | 2021-06-13T08:10:15Z | - |
| dc.date.available | 2005-07-26 | |
| dc.date.copyright | 2005-07-26 | |
| dc.date.issued | 2005 | |
| dc.date.submitted | 2005-07-20 | |
| dc.identifier.citation | 林怡岑 (2003) 甘藷塊根磷解脢與proteasome之結合與降解關係 碩士論文 國立台灣大學 台北
林俊毅 (2002) 建立紅麴毒素citrin酵素免疫分析法之研究 碩士論文 國立台灣大學 台北 吳其真 (1998) 甘藷澱粉磷解脢之生化及免疫學研究 碩士論文 國立台灣大學 台北 陳家裕 (1995) 甘藷中H型澱粉磷解脢的純化及性質研究 碩士論文 國立台灣大學 台北 陳翰民 (1997) 甘藷澱粉磷解脢構造與功能之研究 博士論文 國立台灣大學 台北 張世宗 (1999) 甘藷塊根chaperonin及proteasome之分離與性質研究 博士論文 國立台灣大學 台北 莊榮輝 (1985) 水稻蔗糖合成脢之研究 博士論文 國立台灣大學 台北 Ahmad Z, Huang KP (1981) Dephosphorylation of rabbit skeletal muscle glycogen synthase (phosphorylated by cyclic AMP-independent synthase kinase 1) by phosphatases. J Biol Chem 256: 757-760 Akazawa T, Nelson OE (1966) Starch granule-bound adenosine diphosphate glucose-starch glucosyltransferases of maize seeds. J Biol Chem 241: 2280-2285 Albrecht T, Koch A, Lode A, Greve B, Schneider-Mergener J, Steup M (2001) Plastidic (Pho1-type) phosphorylase isoforms in potato (Solanum tuberosum L.) plants: expression analysis and immunochemical characterization. Planta 213: 602-613 Albrecht T, Greve B, Pusch K, Kossmann J, Buchner P, Wobus U, Steup M (1998) Homodimers and heterodimers of Pho1-type phosphorylase isoforms in Solanum tuberosum L. as revealed by sequence-specific antibodies. Eur J Biochem 251: 343-352 Allen JF (1992) How does protein phosphorylation regulate photosynthesis? Trends Biochem Sci 17: 12-17 Andreassen PR, Lacroix FB, Villa-Moruzzi E, Margolis RL (1998) Differential subcellular localization of protein phosphatase-1 alpha, gamma1, and delta isoforms during both interphase and mitosis in mammalian cells. J Cell Biol 141: 1207-1215 Angosto T, Matilla A (1990) Partial purification and some biochemical properties of nonspecific alkaline phosphatase in germinating chickpea (Cicer arietinum) seeds. Physiol Plant 80: 136-142 Armstrong RN, Kondo H, Granot J, Kaiser ET, Mildvan AS (1979) Magnetic resonance and kinetic studies of the manganese(II) ion and substrate complexes of the catalytic subunit of adenosine 3',5'-monophosphate dependent protein kinase from bovine heart. Biochemistry 18: 1230-1238 Asano T, Kunieda N, Omura Y, Ibe H, Kawasaki T, Takano M, Sato M, Furuhashi H, Mujin T, Takaiwa F, Wu Cy CY, Tada Y, Satozawa T, Sakamoto M, Shimada H (2002) Rice SPK, a calmodulin-like domain protein kinase, is required for storage product accumulation during seed development: phosphorylation of sucrose synthase is a possible factor. Plant Cell 14: 619-628 Ball SG, Guan HP, James M, Myers A, Keeling P, Mouille G, Buleon A, Colonna P, Preiss J (1996) From glycogen to amylopectin: a model for the biogenesis of the plant starch granule. Cell 86: 349-352 Ball SG, Morell MK (2003) From bacterial glycogen to starch: understanding the biogenesis of the plant starch granule. Annu Rev Plant Biol 54: 207-233 Barford D (1995) Protein phosphatases. Curr Opin Struct Biol 5: 728-734 Barford D (1996) Molecular mechanisms of the protein serine/threonine phosphatases. Trends Biochem Sci 21: 407-412 Bender J, Fink GR (1994) AFC1, a LAMMER kinase from Arabidopsis thaliana, activates STE12-dependent processes in yeast. Proc Natl Acad Sci U S A 91: 12105-12109 Bennett J (1980) Chloroplast phosphoproteins. Evidence for a thylakoid-bound phosphoprotein phosphatase. Eur J Biochem 104: 85-89 Bennett J (1991) Phosphorylation in green plant chloroplast. Annu Rev Plant Physiol Plant Mol Biol 42: 281-331 Bieleski RL, Ferguson IB (1983) Physiology and metabolism of phosphate and its compounds. In: Lauchli A, Bieleski RL (eds) Encyclopedia of plant physiology, NS, vol 15A. Springer, Berlin Heidelberg New York, pp 422-449 Bleecker AB, Schaller GE (1996) The Mechanism of Ethylene Perception. Plant Physiol 111: 653-660 Boyle WJ, van der GP, Hunter T (1991) Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol 201: 110-149 Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254 Braun DM, Walker JC (1996) Plant transmembrane receptors: new pieces in the signaling puzzle. Trends Biochem Sci 21: 70-73 Brewis ND, Street AJ, Prescott AR, Cohen PT (1993) PPX, a novel protein serine/threonine phosphatase localized to centrosomes. EMBO J 12: 987-996 Browner MF, Fletterick RJ (1992) Phosphorylase: a biological transducer. Trends Biochem Sci 17: 66-71 Buchner P, Borisjuk L, Wobus U (1996) Glucan phosphorylases in Vicia faba L.: cloning, structural analysis and expression patterns of cytosolic and plastidic forms in relation to starch. Planta 199: 64-73 Budde RJ, Ramdas L, Ke S (1993) Recombinant pp60c-src from baculovirus-infected insect cells: purification and characterization. Prep Biochem 23: 493-515 Burnett G, Kennedy EP (1954) The enzymatic phosphorylation of proteins. J Biol Chem 211: 969-980 Burr B, Nelson OE (1975) Maize alpha-glucan phosphorylase. Eur J Biochem 56: 539-546 Chang C, Kwok SF, Bleecker AB, Meyerowitz EM (1993) Arabidopsis ethylene-response gene ETR1: similarity of product to two-component regulators. Science 262: 539-544 Chen HM, Chang SC, Wu CC, Cuo TS, Wu JS, Juang RH (2002) Regulation of the catalytic behaviour of L-form starch phosphorylase from sweet potato roots by proteolysis. Physiol Plant 114: 506-515 Cheng SH, Willmann MR, Chen HC, Sheen J (2002) Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family. Plant Physiol 129: 469-485 Clark KL, Larsen PB, Wang X, Chang C (1998) Association of the Arabidopsis CTR1 Raf-like kinase with the ETR1 and ERS ethylene receptors. Proc Natl Acad Sci U S A 95: 5401-5406 Cohen PT (1989) The structure and regulation of protein phosphatases. Annu Rev Biochem 58: 453-508 Cohen PT (1997) Novel protein serine/threonine phosphatases: variety is the spice of life. Trends Biochem Sci 22: 245-251 Collinge MA, Walker JC (1994) Isolation of an Arabidopsis thaliana casein kinase II beta subunit by complementation in Saccharomyces cerevisiae. Plant Mol Biol 25: 649-658 Cori CF, Cori GT (1931) Mechanism of formation of hexosemonophosphate in muscle and isolation of a new phosphate ester. Proc Soc Exp Biol Med 34: 702-703 Czernic P, Visser B, Sun W, Savoure A, Deslandes L, Marco Y, Van Montagu M, Verbruggen N (1999) Characterization of an Arabidopsis thaliana receptor-like protein kinase gene activated by oxidative stress and pathogen attack. Plant J 18: 321-327 Da Mota RV, Cordenunsi BR, Do N, Jr., Purgatto E, Rosseto MR, Lajolo FM (2002) Activity and expression of banana starch phosphorylases during fruit development and ripening. Planta 216: 325-333 Da Cruz e Silva OB, Da Cruz e Silva EF, Cohen PT (1988) Identification of a novel protein phosphatase catalytic subunit by cDNA cloning. FEBS Lett 242: 106-110 Dale S, Wilson WA, Edelman AM, Hardie DG (1995) Similar substrate recognition motifs for mammalian AMP-activated protein kinase, higher plant HMG-CoA reductase kinase-A, yeast SNF1, and mammalian calmodulin-dependent protein kinase I. FEBS Lett 361: 191-195 Duwenig E, Steup M, Kossmann J (1997) Induction of genes encoding plastidic phosphorylase from spinach (Spinacia oleracea L.) and potato (Solanum tuberosum L.) by exogenously supplied carbohydrates in excised leaf discs. Planta 203: 111-120 Duwenig E, Steup M, Willmitzer L, Kossmann J (1997) Antisense inhibition of cytosolic phosphorylase in potato plants (Solanum tuberosum L.) affects tuber sprouting and flower formation with only little impact on carbohydrate metabolism. Plant J 12: 323-333 Ferreira PC, Hemerly AS, Villarroel R, Van Montagu M, Inze D (1991) The Arabidopsis functional homolog of the p34cdc2 protein kinase. Plant Cell 3: 531-540 Fiske C, Subbarow Y (1925) The colourimetric determination of phosphorus. J Biol Chem 66: 375-400 Fletterick RJ, Sygusch J, Murray N, Madsen NB (1976) Low-resolution structure of the glycogen phosphorylase alpha monomer and comparison with phosphorylase beta. J Mol Biol 103: 1-13 Flinta C, von Heijne G, Johansson J (1983) Helical sidedness and the distribution of polar residues in trans-membrane helices. J Mol Biol 168: 193-196 Frydman RB, Cardini CE (1964) Biosynthesis of phytoglycogen from adenosine diphosphate D-glucose in sweet corn. Biochem Biophys Res Commun 14: 353-357 Fukui T, Shimomura S, Nakano K (1982) Potato and rabbit muscle phosphorylases: comparative studies on the structure, function and regulation of regulatory and nonregulatory enzymes. Mol Cell Biochem 42: 129-144 Fukui T (1983) Plant phosphorylase: structure and function. In T Akazawa, T Asahi, He Imaseki, eds, The New Frontiers in Plant Biochemistry, Ed Japan Scientific Societies Press Tokyo, pp 71-82 Fukui T, Nakano K, Tagaya M, Nakayma H (1987) Phosphorylase isozymes of higher plants. In Biochemistry of Vitamin B6 , (Korpela,T.and Christen,P.,eds), Basel: Birkhauser Verlag, pp 267-276 Gerbrandy SJ, Shankar V, Shivaram KN, Stegemann H (1975) Conversion of potato phosphorylase isozymes. Phytochemistry 14: 2331-2333 Guan KL, Dixon JE (1990) Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia. Science 249: 553-556 Halford NG, Hardie DG (1998) SNF1-related protein kinases: global regulators of carbon metabolism in plants? Plant Mol Biol 37: 735-748 Hanes CS (1940a) The reversible formation of starch from glucose -1-phosphate catalyzed by potato phosphorylase. Proc R Soc (London) B129: 174-208 Hanes CS (1940b) The breakdown and synthesis of starch by an enzyme system from pea seeds. Proc Roy Soc (London) B128: 421-500 Hanks SK, Quinn AM (1991) Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol 200: 38-62 Hanks SK, Hunter T (1995) Protein Kinases .6. the Eukaryotic Protein-Kinase Superfamily - Kinase (Catalytic) Domain-Structure and Classification. Faseb Journal 9: 576-596 Hardie DG (1999) PLANT PROTEIN SERINE/THREONINE KINASES: Classification and Functions. Annu Rev Plant Physiol Plant Mol Biol 50: 97-131 Harmon AC (1989) Protein Kinases in Soybean Nuclei. Plant Cell 1: 745 Hao L, Wang H, Sunter G, Bisaro DM (2003) Geminivirus AL2 and L2 proteins interact with and inactivate SNF1 kinase. Plant Cell 15: 1034-1048 He ZH, Fujiki M, Kohorn BD (1996) A cell wall-associated, receptor-like protein kinase. J Biol Chem 271: 19789-19793 He ZH, Cheeseman I, He D, Kohorn BD (1999) A cluster of five cell wall-associated receptor kinase genes, Wak1-5, are expressed in specific organs of Arabidopsis. Plant Mol Biol 39: 1189-1196 Heldt H.W., Chou C.H., Maronde D., Herold A., Stankovic Z.S., Kraminer A., Kirk M.R., Heber U. (1977) Role of orthophosphate and other factors in regulation of starch formation in leaves and isolated-chloroplasts. Plant Physiol 55: 1146-1155 Herve C, Dabos P, Galaud JP, Rouge P, Lescure B (1996) Characterization of an Arabidopsis thaliana gene that defines a new class of putative plant receptor kinases with an extracellular lectin-like domain. J Mol Biol 258: 778-788 Hidaka H, Kobayashi R (1994) Protein kinase inhibitors. Essays Biochem 28: 73-97 Hirayama T, Imajuku Y, Anai T, Matsui M, Oka A (1991) Identification of two cell-cycle-controlling cdc2 gene homologs in Arabidopsis thaliana. Gene 105: 159-165 Hirayama T, Oka A (1992) Novel protein kinase of Arabidopsis thaliana (APK1) that phosphorylates tyrosine, serine and threonine. Plant Mol Biol 20: 653-662 Hirt H (2000) MAP kinases in plant signal transduction. Results Probl Cell Differ 27: 1-9 Hirt H (1997) Multiple roles of MAP kinases in plant signal transduction. Trends Plant Sci 2: 11-15 Huala E, Oeller PW, Liscum E, Han IS, Larsen E, Briggs WR (1997) Arabidopsis NPH1: a protein kinase with a putative redox-sensing domain. Science 278: 2120-2123 Hwang I, Goodman HM (1995) An Arabidopsis thaliana root-specific kinase homolog is induced by dehydration, ABA, and NaCl. Plant J 8: 37-43 Ichimura K, Mizoguchi T, Irie K, Morris P, Giraudat J, Matsumoto K, Shinozaki K (1998) Isolation of ATMEKK1 (a MAP kinase kinase kinase)-interacting proteins and analysis of a MAP kinase cascade in Arabidopsis. Biochem Biophys Res Commun 253: 532-543 Ito T, Takahashi N, Shimura Y, Okada K (1997) A serine/threonine protein kinase gene isolated by an in vivo binding procedure using the Arabidopsis floral homeotic gene product, AGAMOUS. Plant Cell Physiol 38: 248-258 Johnson LN, Barford D (1990) Glycogen phosphorylase. The structural basis of the allosteric response and comparison with other allosteric proteins. J Biol Chem 265: 2409-2412 Jonak C, Hirt H (2002) Glycogen synthase kinase 3/SHAGGY-like kinases in plants: an emerging family with novel functions. Trends Plant Sci 7: 457-461 Juang RH, Chang YD, Sung HY, Su JC (1984) Oven-drying method for polyacrylamide gel slab packed in cellophane sandwich. Anal Biochem 141: 348-350 Kakimoto T (1998) Cytokinin signaling. Curr Opin Plant Biol 1: 399-403 Kemp BE, Pearson RB (1990) Protein kinase recognition sequence motifs. Trends Biochem Sci 15: 342-346 Kennelly PJ, Krebs EG (1991) Consensus sequences as substrate specificity determinants for protein kinases and protein phosphatases. J Biol Chem 266: 15555-15558 Kerk D, Bulgrien J, Smith DW, Barsam B, Veretnik S, Gribskov M (2002) The complement of protein phosphatase catalytic subunits encoded in the genome of Arabidopsis. Plant Physiol 129: 908-925 Kerbs EG, Kent AB, Fischer EH (1958) The muscle phosphorylase b kinase reaction. J Biol Chem 231: 73-83 Kieber JJ, Rothenberg M, Roman G, Feldmann KA, Ecker JR (1993) CTR1, a negative regulator of the ethylene response pathway in Arabidopsis, encodes a member of the raf family of protein kinases. Cell 72: 427-441 Klimczak LJ, Farini D, Lin C, Ponti D, Cashmore AR, Giuliano G (1995) Multiple isoforms of Arabidopsis casein kinase I combine conserved catalytic domains with variable carboxyl-terminal extensions. Plant Physiol 109: 687-696 Knetsch M, Wang M, Snaar-Jagalska BE, Heimovaara-Dijkstra S (1996) Abscisic Acid Induces Mitogen-Activated Protein Kinase Activation in Barley Aleurone Protoplasts. Plant Cell 8: 1061-1067 Knowles JR (1980) Enzyme-catalyzed phosphoryl transfer reactions. Annu Rev Biochem 49: 877-919 Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685 Lawson JE, Niu XD, Browning KS, Trong HL, Yan J, Reed LJ (1993) Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C. Biochemistry 32: 8987-8993 Lawton MA, Yamamoto RT, Hanks SK, Lamb CJ (1989) Molecular cloning of plant transcripts encoding protein kinase homologs. Proc Natl Acad Sci U S A 86: 3140-3144 Leloir LF, De Fekete MA, Cardini CE (1961) Starch and oligosaccharide synthesis from uridine diphosphate glucose. J Biol Chem 236: 636-641 Lin CT, Yeh KW, Lee PD, Su JC (1991) Primary structure of sweet potato starch phosphorylase deduced from its cDNA sequence. Plant Physiol 95: 1250-1253 Luan S (2003) Protein phosphatases in plants. Annu Rev Plant Biol 54: 63-92 MacKintoch C, Coggins J, Cohen P (1991) Plant protein phosphatase: subcellular distribution, detection of protein phosphatase 2Cand identification of protein phosphatase 2A as the major quinate dehydrogenase phosphatase. Biochem J 273: 733-738 Matte A, Tari LW, Delbaere LT (1998) How do kinases transfer phosphoryl groups? Structure 6: 413-419 Mikolajczyk M, Awotunde OS, Muszynska G, Klessig DF, Dobrowolska G (2000) Osmotic stress induces rapid activation of a salicylic acid-induced protein kinase and a homolog of protein kinase ASK1 in tobacco cells. Plant Cell 12: 165-178 Mildvan AS, Rosevear PR, Fry DC, Bramson HN, Kaiser ET (1985) NMR studies of the mechanism of action and regulation of protein kinase. Curr Top Cell Regul 27: 133-144 Mizoguchi T, Hayashida N, Yamaguchi-Shinozaki K, Kamada H, Shinozaki K (1995) Two genes that encode ribosomal-protein S6 kinase homologs are induced by cold or salinity stress in Arabidopsis thaliana. FEBS Lett 358: 199-204 Mizoguchi T, Yamaguchi-Shinozaki K, Hayashida N, Kamada H, Shinozaki K (1993) Cloning and characterization of two cDNAs encoding casein kinase II catalytic subunits in Arabidopsis thaliana. Plant Mol Biol 21: 279-289 Moran TV, Walker JC (1993) Molecular cloning of two novel protein kinase genes from Arabidopsis thaliana. Biochim Biophys Acta 1216: 9-14 Mori H, Tanizawa K, Fukui T (1991) Potato tuber type H phosphorylase isozyme. Molecular cloning, nucleotide sequence, and expression of a full-length cDNA in Escherichia coli. J Biol Chem 266: 18446-18453 Mori H, Tanizawa K, Fukui T (1993) A chimeric alpha-glucan phosphorylase of plant type L and H isozymes. Functional role of 78-residue insertion in type L isozyme. J Biol Chem 268: 5574-5581 Muller-Rober B, Sonnewald U, Willmitzer L (1992) Inhibition of the ADP-glucose pyrophosphorylase in transgenic potatoes leads to sugar-storing tubers and influences tuber formation and expression of tuber storage protein genes. EMBO J 11: 1229-1238 Nakano K, Fukui T (1986) The complete amino acid sequence of potato alpha-glucan phosphorylase. J Biol Chem 261: 8230-8236 Nakano K, Mori H, Fukui T (1989) Molecular cloning of cDNA encoding potato amyloplast alpha-glucan phosphorylase and the structure of its transit peptide. J Biochem (Tokyo) 106: 691-695 Neel BG, Tonks NK (1997) Protein tyrosine phosphatases in signal transduction. Curr Opin Cell Biol 9: 193-204 Ogawara H, Akiyama T, Ishida J, Watanabe S, Suzuki K (1986) A specific inhibitor for tyrosine protein kinase from Pseudomonas. J Antibiot (Tokyo) 39: 606-608 Parkinson JS (1993) Signal transduction schemes of bacteria. Cell 73: 857-871 Pinna LA, Ruzzene M (1996) How do protein kinases recognize their substrates? Biochim Biophys Acta 1314: 191-225 Prade L, Engh RA, Girod A, Kinzel V, Huber R, Bossemeyer D (1997) Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential. Structure 5: 1627-1637 Preiss J, Greenberg E (1967) Biosynthesis of starch in Chlorella pyrenoidosa. I. Purification and properties of the adenosine diphosphoglucose: alpha-1, 4-glucan, alpha-4-glucosyl transferase from Chlorella. Arch Biochem Biophys 118: 702-708 Preiss J., Levi C. (1979) Metabolism of starch in leaves. Encyclopedia of Plant Physiology, New York, pp 282-312 Preiss J, Okita TW, Greenberg E (1980) Characterization of the spinach leaf phosphorylase. Plant Physiol 66: 864-869 Quail PH (1997) The phytochromes: a biochemical mechanism of signaling in sight? Bioessays 19: 571-579 Raghavan S, Williams I, Aslam H, Thomas D, Szoor B, Morgan G, Gross S, Turner J, Fernandes J, VijayRaghavan K, Alphey L (2000) Protein phosphatase 1beta is required for the maintenance of muscle attachments. Curr Biol 10: 269-272 Richardson RH, Matheson N.K. (1977) Some molecular properties of plant starch phosphorylases and the levels of activity of the multiple forms. Phytochemistry 16: 1875-1879 Roe JL, Rivin CJ, Sessions RA, Feldmann KA, Zambryski PC (1993) The Tousled gene in A. thaliana encodes a protein kinase homolog that is required for leaf and flower development. Cell 75: 939-950 Rogers S, Wells R, Rechsteiner M (1986) Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234: 364-368 Savaldi-Goldstein S, Aviv D, Davydov O, Fluhr R (2003) Alternative splicing modulation by a LAMMER kinase impinges on developmental and transcriptome expression. Plant Cell 15: 926-938 Schillace RV, Scott JD (1999) Association of the type 1 protein phosphatase PP1 with the A-kinase anchoring protein AKAP220. Curr Biol 9: 321-324 Schmidt HA, Strimmer K, Vingron M, von Haeseler A (2002) TREE-PUZZLE: maximum likelihood phylogenetic analysis using quartets and parallel computing. Bioinformatics 18: 502-504 Schneider EM, Becker JU, Volkmann D (1979) The role of phosphorylase in plant storage tissue studied by immunological methods. Hoppe Seylers Z Physiol Chem 960: 369-370 Schneider EM, Becker JU, Volkmann D (1981) Biochemical properties of potato phosphorylase change with its intracellular localization as revealed by immunological methods. Planta 151: 124-134 Sheen J (1996) Ca2+-dependent protein kinases and stress signal transduction in plants. Science 274: 1900-1902 Shenolikar S (1994) Protein serine/threonine phosphatases--new avenues for cell regulation. Annu Rev Cell Biol 10: 55-86 Shimomura S, Nagai M, Fukui T (1982) Comparative glucan specificities of two types of spinach leaf phosphorylase. J Biochem (Tokyo) 91: 703-717 Shiu SH, Bleecker AB (2003) Expansion of the receptor-like kinase/Pelle gene family and receptor-like proteins in Arabidopsis. Plant Physiol 132: 530-543 Silverstein T, Cheng L, Allen JF (1993) Chloroplast thylakoid protein phosphatase reactions are redox-independent and kinetically heterogeneous. FEBS Lett 334: 101-105 Sonnewald U, Basner A, Greve B, Steup M (1995) A second L-type isozyme of potato glucan phosphorylase: cloning, antisense inhibition and expression analysis. Plant Mol Biol 27: 567-576 Steup M (1981) Purification of chloroplast alpha-1,4-glucan phosphorylase from spinach leaves by chromatography on Sepharose-bound starch. Biochim Biophys Acta 659: 123-131 Steup M (1988) Starch degradation. In J. Preiss, ed, The Biochemistry of Plants, Vol 14. Academic Press, San Diego, CA, pp 255-296 Stone RL, Dixon JE (1994) Protein-tyrosine phosphatases. J Biol Chem 269: 31323-31326 Sugden C, Donaghy PG, Halford NG, Hardie DG (1999) Two SNF1-related protein kinases from spinach leaf phosphorylate and inactivate 3-hydroxy-3-methylglutaryl-coenzyme A reductase, nitrate reductase, and sucrose phosphate synthase in vitro. Plant Physiol 120: 257-274 Sun G, Budde RJ (1997) Requirement for an additional divalent metal cation to activate protein tyrosine kinases. Biochemistry 36: 2139-2146 Sun G, Markwell J (1992) Lack of type 1 and type 2A protein serine (P)/threonine (P) phosphatase activities in chloroplast. Plant Physiol 100: 620-624 Tanase K, Shiratake K, Mori H, Yamaki S (2002) Changes in the phosphorylation state of sucrose synthase during development of Japanese pear fruit. Physiol Plant 114: 21-26 Tetlow IJ, Wait R, Lu Z, Akkasaeng R, Bowsher CG, Esposito S, Kosar-Hashemi B, Morell MK, Emes MJ (2004) Protein phosphorylation in amyloplasts regulates starch branching enzyme activity and protein-protein interactions. Plant Cell 16: 694-708 Thelen JJ, Miernyk JA, Randall DD (1998) Partial purification and characterization of the maize mitochondrial pyruvate dehydrogenase complex. Plant Physiol 116: 1443-1450 Turck F, Kozma SC, Thomas G, Nagy F (1998) A heat-sensitive Arabidopsis thaliana kinase substitutes for human p70s6k function in vivo. Mol Cell Biol 18: 2038-2044 Uehara K, Fujimoto S, Taniguchi T (1974) Studies on violet-colored acid phosphatase of sweet potato. I. Purification and some physical properties. J Biochem (Tokyo) 75: 627-638 Uehara K, Fujimoto S, Taniguchi T, Nakai K (1974) Studies on violet-colored acid phosphatase of sweet potato. II. Enzymatic properties and amino acid composition. J Biochem (Tokyo) 75: 639-649 Urao T, Yakubov B, Satoh R, Yamaguchi-Shinozaki K, Seki M, Hirayama T, Shinozaki K (1999) A transmembrane hybrid-type histidine kinase in Arabidopsis functions as an osmosensor. Plant Cell 11: 1743-1754 Walker JC (1994) Structure and function of the receptor-like protein kinases of higher plants. Plant Mol Biol 26: 1599-1609 Yamada K, Lim J, Dale JM, Chen H, Shinn P, Palm CJ, Southwick AM, Wu HC, Kim C, Nguyen M, Pham P, Cheuk R, Karlin-Newmann G, Liu SX, Lam B, Sakano H, Wu T, Yu G, Miranda M, Quach HL, Tripp M, Chang CH, Lee JM, Toriumi M, Chan MM, Tang CC, Onodera CS, Deng JM, Akiyama K, Ansari Y, Arakawa T, Banh J, Banno F, Bowser L, Brooks S, Carninci P, Chao Q, Choy N, Enju A, Goldsmith AD, Gurjal M, Hansen NF, Hayashizaki Y, Johnson-Hopson C, Hsuan VW, Iida K, Karnes M, Khan S, Koesema E, Ishida J, Jiang PX, Jones T, Kawai J, Kamiya A, Meyers C, Nakajima M, Narusaka M, Seki M, Sakurai T, Satou M, Tamse R, Vaysberg M, Wallender EK, Wong C, Yamamura Y, Yuan S, Shinozaki K, Davis RW, Theologis A, Ecker JR (2003) Empirical analysis of transcriptional activity in the Arabidopsis genome. Science 302: 842-846 Yu Y, Mu HH, Wasserman BP, Carman GM (2001) Identification of the maize amyloplast stromal 112-kD protein as a plastidic starch phosphorylase. Plant Physiol 125: 351-359 Zeeman SC, Thorneycroft D, Schupp N, Chapple A, Weck M, Dunstan H, Haldimann P, Bechtold N, Smith AM, Smith SM (2004) Plastidial {alpha}-Glucan Phosphorylase Is Not Required for Starch Degradation in Arabidopsis Leaves But Has a Role in the Tolerance of Abiotic Stress. Plant Physiol 135: 849-858 Zeeman SC, Northrop F, Smith AM, Rees T (1998) A starch-accumulating mutant of Arabidopsis thaliana deficient in a chloroplastic starch-hydrolysing enzyme. Plant J 15: 357-365 Zhang S, Du H, Klessig DF (1998) Activation of the tobacco SIP kinase by both a cell wall-derived carbohydrate elicitor and purified proteinaceous elicitins from Phytophthora spp. Plant Cell 10: 435-450 Zhang SH, Lawton MA, Hunter T, Lamb CJ (1994) atpk1, a novel ribosomal protein kinase gene from Arabidopsis. I. Isolation, characterization, and expression. J Biol Chem 269: 17586-17592 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/36668 | - |
| dc.description.abstract | 甘藷塊根L型澱粉磷解脢 (L-SP, EC 2.4.1.1) 中央序列 (L78) 斷裂後，可提高對於澱粉的親和力。以電腦程式PC/GENE分析L78，預測此序列包含有一段易受到蛋白脢攻擊的PEST site以及數個可能受到磷酸化修飾的位置。本論文利用純化自甘藷塊根L-SP作為基質，篩選甘藷塊根蛋白質中可對L-SP進行磷酸化作用的激脢。根據專一性免疫沈澱法的實驗結果顯示：L-SP確實可受到甘藷塊根中內生性鎂或錳需求型蛋白質激脢的磷酸化修飾，因此利用硫酸銨分劃以及三種不同性質的管柱層析法，將此一激脢自甘藷塊根粗抽液中純化分離至部份均質，命名為L型澱粉磷解脢激脢 (LSK)。將LSK以Native/SDS二次元電泳解析，再配合質譜儀鑑定，發現當中含有顯著Ser/Thr蛋白質激脢訊號。此一激脢的原態分子量，經膠體過濾法以及膠體內激脢分析法估計為338 kD。LSK的活性可受到蛋白質激脢抑制劑staurosporine的抑制，而L-SP的磷酸化可被來自於牛腸胃道的鹼性磷酸脢去磷酸化。使用不同的L-SP片段作為LSK的基質，發現LSK針對含有L-SP中央序列的表現蛋白質L78P作用。磷酸化胺基酸分析結果顯示LSK是針對L78序列的Ser進行磷酸化修飾。針對L78P正常株的定點突變結果，則確認LSK針對L78的Ser527進行磷酸化修飾。磷酸化的L-SP在試管中的結果顯示：L-SP的磷酸化修飾會導致L78的移除，但是並不會改變本身的酵素動力學參數。根據本論文結果顯示：LSK對於L-SP的磷酸化修飾在澱粉代謝中扮演著重要的調節性角色。 | zh_TW |
| dc.description.abstract | The degradation of middle chain (L78) of L-form starch phosphorylase (L-SP, EC 2.4.1.1) from sweet potato roots could increase the binding affinity to soluble starch. The computational analysis of the amino acid sequence on L78 predicted that it contains a proteolytic PEST site and several phosphorylation sites at its Ser residues. We used purified L-SP from sweet potato roots as a substrate to screen the relative protein kinase(s). According to the results of specific immunoprecipitation, we demonstrated that L-SP was phosphorylated in Mg2+ or Mn2+-dependent manner by endogenous protein kinases from sweet potato roots. The protein named L-form starch phosphorylase kinase (LSK) was partial purified from sweet potato roots by ammonium sulfate fractionation, followed by ion-exchange, phosphocellulose, and gel-filtration chromatography. LSK was resolved in a two dimensional native/sodium dodecyl sulfate-polyacrylamide gel electrophoresis system and characterized using liquid chromatography-tandem mass spectrometry. The native molecular mass of the enzyme determined by gel filtration and in-gel kinase assay was 338 kD. The activation of LSK was suppressed by the protein kinase inhibitor staurosporine, and the phosphorylation of L-SP was abolished by calf intestinal alkaline phosphatase. An expressed peptide (L78P) containing the essential part of L78 was phosphorylated by the kinase, but the proteolytic modified L-SP which lost its L78 fragment was not. Phospho-amino acid analysis showed that only serine residues were phosphorylated. Furthermore, using L78P mutants by site-directed mutagenesis at serine residues on L78, we demonstrate that only Ser527 on L78 is phosphorylated by the kinase. In vitro assays of phosphorylated L-SP which was mixed with crude extract from sweet potato roots show that the proteolytic degradation of L78 was introduced by L-SP phosphorylation, but had no change in its kinetic parameters. These results suggest that the phosphorylation of L-SP by LSK plays an important regulatory role in starch metabolism. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-13T08:10:15Z (GMT). No. of bitstreams: 1 ntu-94-D88623603-1.pdf: 5040738 bytes, checksum: bfdbf2176275c5e5d72c9f9fb4d5bb01 (MD5) Previous issue date: 2005 | en |
| dc.description.tableofcontents | 目 錄
目 錄.......................................................................................................................................................2 中文摘要.................................................................................................................................................5 ABSTRACT...........................................................................................................................................7 縮寫表.....................................................................................................................................................8 第一章 概 論.......................................................................................................................................10 1.1 澱粉磷解 ................................................................................................................................10 1.1.1 澱粉磷解 的分類.............................................................................................................10 1.1.2 澱粉磷解 的生理功能.....................................................................................................11 1.2 實驗緣起....................................................................................................................................14 1.2.1 L-SP 序列比較...................................................................................................................15 1.2.2 中央L78 序列分析............................................................................................................19 1.2.3 動物肝醣磷解 與植物澱粉磷解 的比較.....................................................................24 1.2.3 甘藷塊根L-SP 的相關研究進度.......................................................................................25 1.2.4 研究動機............................................................................................................................26 1.3 蛋白質的磷酸化與去磷酸化.....................................................................................................31 1.3.1 植物蛋白質激 .................................................................................................................33 1.3.2 植物蛋白質磷酸 .............................................................................................................42 1.3.3 抑制劑與訊息傳導路徑.....................................................................................................47 1.4 結語............................................................................................................................................52 第二章 甘藷塊根澱粉磷解 激 之純化與分離..............................................................................54 2.1 硫酸銨分劃................................................................................................................................55 2.2 DEAE SEPHACEL .........................................................................................................................57 2.3 CELLULOSE PHOSPHATE ...............................................................................................................58 2.4 SEPHACRYL S-300 ........................................................................................................................59 2.5 PURIFICATION TABLE ....................................................................................................................59 2.6 LC-MS/MS 鑑定LSK 身分.......................................................................................................60 2.7 結論............................................................................................................................................61 第三章 LSK 之生化性質分析.............................................................................................................72 3.1 LSK 是鎂/錳離子依賴型激 ...................................................................................................72 3.2 LSK 最適反應條件.....................................................................................................................74 3 3.3 LSK 原態分子量測定.................................................................................................................75 3.4 專一性SER/THR 蛋白質激 抑制劑對於LSK 活性的影響....................................................77 3.5 L-SP 在試管中可逆式的磷酸化修飾.........................................................................................79 3.6 LSK 對於甘藷塊根內蛋白質的專一性.....................................................................................82 3.7 結論............................................................................................................................................83 第四章 L-SP 的磷酸化位置分析........................................................................................................96 4.1 L78 序列之表現、純化以及單株抗體之製備..........................................................................96 4.2 L-SP 的磷酸化胺基酸種類........................................................................................................97 4.3 L-SP 磷酸化位置........................................................................................................................98 4.4 L-SP 的磷酸化會導致L78 快速降解......................................................................................100 4.5 結論..........................................................................................................................................103 第五章 L-SP 序列與結構分析........................................................................................................... 115 5.1 甘藷塊根L-SP 磷酸化位置.....................................................................................................115 5.2 L-SP 含有SER/THR 蛋白質激 專一性辨識的保守性序列...................................................116 5.3 不同物種間磷解 序列的同質性...........................................................................................117 5.4 L-SP 可能的立體結構..............................................................................................................120 5.5 結論..........................................................................................................................................123 第六章 總 結.....................................................................................................................................129 6.1 本論文的主要成果...................................................................................................................129 6.2 未來研究方向...........................................................................................................................131 第七章 材料與方法............................................................................................................................135 7.1 電泳檢定法...............................................................................................................................135 7.1.1 原態膠體電泳法...............................................................................................................135 7.1.2 SDS 膠體電泳法...............................................................................................................140 7.1.3 製備式電泳與蛋白質溶離...............................................................................................144 7.1.4 膠體染色法.......................................................................................................................147 7.1.5 膠體乾燥及保存................................................................................................................151 7.1.6 蛋白質電泳膠體轉印法...................................................................................................153 7.2 一般分析法...............................................................................................................................155 7.2.1 蛋白質定量.......................................................................................................................155 7.2.2 甘藷塊根澱粉磷解 L-SP 活性分析法.........................................................................157 7.2.3 甘藷澱粉磷解 激 活性分析法...................................................................................159 7.3 管柱色層分析法.......................................................................................................................161 7.3.1 管柱色層分析法基本操作程序.......................................................................................161 7.3.2 膠體使用前處理以及使用後保存...................................................................................165 7.3.3 膠體過濾法.......................................................................................................................165 4 7.3.4 離子交換法.......................................................................................................................167 7.3.5 疏水性層析法...................................................................................................................169 7.3.6 NTA-agarose 親和性層析法............................................................................................171 7.4 免疫學方法...............................................................................................................................173 7.4.1 酵素免疫染色法...............................................................................................................173 7.4.2 放射性酵素免疫染色及顯像法.......................................................................................176 7.4.3 免疫沈澱法.......................................................................................................................177 7.4.4 酵素免疫分析法...............................................................................................................178 7.5 酵素粗抽取及硫酸銨沈澱法...................................................................................................179 7.6 甘藷塊根L 型澱粉磷解 純化法..........................................................................................182 7.7 甘藷塊根L 型澱粉磷解 激 純化法...................................................................................184 7.8 磷酸化胺基酸檢定...................................................................................................................186 7.9 蛋白質N-端序列決定法..........................................................................................................188 7.10 膠體內蛋白 水解.................................................................................................................190 7.11 單株抗體之製備.....................................................................................................................193 7.11.1 動物免疫.........................................................................................................................193 7.11.2 細胞融合.........................................................................................................................195 7.11.3 細胞保存法......................................................................................................................203 7.11.4 單株抗體的生產.............................................................................................................205 7.11.5 免疫球蛋白之純化.........................................................................................................206 7.12 大腸桿菌表現蛋白質L78P 之誘導與純化..........................................................................207 7.13 膠體內激 分析.....................................................................................................................211 7.14 馬鈴薯塊莖L 型澱粉磷解 純化法....................................................................................213 參考文獻.............................................................................................................................................216 問答錄.................................................................................................................................................224 | |
| dc.language.iso | zh-TW | |
| dc.subject | 澱粉磷解脢 | zh_TW |
| dc.subject | 甘藷 | zh_TW |
| dc.subject | 蛋白質激脢 | zh_TW |
| dc.subject | 蛋白質磷酸化 | zh_TW |
| dc.subject | 甘藷塊根 | zh_TW |
| dc.subject | Starch phosphorylase | en |
| dc.subject | Ipomoea batatas | en |
| dc.subject | Protein kinase | en |
| dc.subject | Protein phosphorylation | en |
| dc.subject | Sweet potato roots | en |
| dc.title | 甘藷塊根L型澱粉磷解脢激脢之純化與性質分析 | zh_TW |
| dc.title | The Purification and Functional Assay of L-Form Starch Phosphorylase Kinase from Sweet Potato Roots | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 93-2 | |
| dc.description.degree | 博士 | |
| dc.contributor.oralexamcommittee | 黃鵬林,林耀輝,林棋財,王愛玉,楊健志,陳翰民 | |
| dc.subject.keyword | 甘藷,蛋白質激脢,蛋白質磷酸化,甘藷塊根,澱粉磷解脢, | zh_TW |
| dc.subject.keyword | Ipomoea batatas,Protein kinase,Protein phosphorylation,Sweet potato roots,Starch phosphorylase, | en |
| dc.relation.page | 152 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2005-07-21 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 微生物與生化學研究所 | zh_TW |
| 顯示於系所單位： | 微生物學科所 | |
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