請用此 Handle URI 來引用此文件:
http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75884完整後設資料紀錄
| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.author | 吳素幸 | zh_TW |
| dc.date.accessioned | 2021-07-01T08:16:10Z | - |
| dc.date.available | 2021-07-01T08:16:10Z | - |
| dc.date.issued | 1992 | |
| dc.identifier.citation | 1. Amir-Shapira, D., Leustek, T., Dalie, B., Weissbach, H., Brot, N. 1990 HSP70 proteins, similar to Escherichia coli DnaK, in chloroplasts and mitochondria of Euglena gracil is. Proc. Natl. Acad. Sci. USA 87:1749-52 2. Bardwell, J.C.A., Craig, E.A. 1984. Major heat shock gene of Drosophila and Escherichia coli heat-inducible dnaK gene are homologous. Proc. Natl. Acad. Sci. USA 81:848-52 3. Beckmann, R.P., Mizzen, L.A., Welch, W.J. 1990. Interaction of Hsp70 with newly synthesized proteins: Implications for protein folding and assembly. Science 248:850-54 4. Bernstein, H. D., Poritz, M. A., Strub, K., Hoben, P.J., Brenner, S., Walter, P. 1989. Model for signal sequence recognition from amino-acid sequences of 54K subunit of signal recognition particle. Nature 340:482-86 5. Borkovich, K.A., Farrelly, F.W., Finkelstein, D.B., Taulien, H., Lindquist, S.L. 1989. hsp82 is an essential protein that is rewuired in higher concentrations for growth of cells at high temperatures. Mol. Cell. Biol. 9:3919-30 6. Chappell, T.G., Konforti, B.B., Schmid, S.L., Rothman, J.E. 1987. The ATPase core of a clathrin unscoating protein. J. Biol. Chem. 262:746-51 7. Chen, Q., Lauzon, L., DeRocher, A., Vierling, E. 1990. Accumulation, Stability, and localization of a major chloroplast heat shock protein. J. Cell Biol. 110:1873-83 8. Chen, Q., Vierling, E. 1991. Analysis of conserved domains identifies a unique structural feature of a chloroplast heat shock protein. Mol. Gen. Genet. 9. Cheng, M.Y., Hartl, F.-U., Martin, J., Pollock, R.A., Kalousek, F., et al. 1989. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337:620-25 10. Chirico, W.J., Waters, M.G., Blobel, G. 1988. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature 332: 805-10 11. Chou. M., Chen, Y.-M., Lin, C.-Y. 1989. Thermotolerance of isolated mitochondria associated with heat shock proteins. Plant Physiol. 89:617-21 12. Conner, T.W., LaFayette, P.R., Nagao, R.T., Key, J.L. 1990. Sequence and expression of a HSP83 from Arabidopsis tha-liana. Plant Physiol. 94:1689-95 13. Cooper. P., Ho, T.-H. D. 1987. Intracellular localization of heat shock proteins in maize. Plant Physiol. 84:1197-203 14. Craig, E.A., Kramer, J., Shilling, J., Werner-Washburne, M., Holmes, S., et al. 1989. SSC1, an essential member of the yeast HSP70 multigene family encodes a mitochondrial protein. Mol. Cell. Biol. 9:3000-8 15. Czarnecka, E., Gurley, W.B., Nagao, R.T., Mosquera, L.A., Key, J.L. 1985. DNA sequence and transcript mapping of a soybean gene encoding a small heat shock protein. Proc. Natl. Acad. Sci. USA 82:3726-30 16. DeLuca-Flaherty, C., McKay, D.B., Parham, P., Hill, B.L. 1990. Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis. Cell 62:875-87 17. DeRocher, A., Lauzon, L., Vierling, E. 1990. HSP70 expression during seed development. J. Cell. Biochem. 14E:298 (Abstr.) 18. Deshaies, R.J., Koch, B.D., Werner-Washburne, M., Craig, E.A., Schekman, R. 1988. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332:800-5 19. Duck, N., McCormick, S., Winter, J. 1989. Heat Shock protein hsp70 cognate expression in vegetative and reproductive organs of Lycopersicon esculentum. Proc. Natl. Acad. Sci. USA 86:3674-78 20. Ellis, J. 1987. Proteins as molecular chaperones. Nature 328:378-79 21. Engman, D.M., Kirchhoff, L.V., Donelson, J.E. 1989. Molecular cloning of mtp70, a metochondrial member of the hsp70 family. Mol. Cell. Biol. 9:5163-68 22. Flaherty, K.M., DeLuca-Flaherty, C., McKay, D.B. 1990. Three-dimentional structure of the ATPase fragment of a 70K heat -shock cognate protein. Nature 346:623-28 23. Flynn, G.C., Chappell, T.G., Rothman, J.E. 1989. Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 245:385-90 24. Gaitanaris, G.A., Papavassiliou, A.G., Rubock, P., Silverstein, S.J., Gottesman, M.E. 1990. Renaturation of lambda repressor requires heat shock proteins. Cell 61: 1013-20 25. Helm, K.W., Vierling, E. 1990. A member of the eukaryoric superfamily of small heat shock proteins is located in the endomembrane system of Pisum sativum. J. Cell Biol. 111:69a 26. Hemmingsen, S.M., Woolford, C., vander Vies, S.M., Tilly, K., Dennis, D.T. 1988. Homologous plant and bacterial proteins chaperone oligomeric ptotein assembly. Nature 333: 330-3426. 27. Hsieh, M.H., Chen, J.T., Jinn, T.L., Chen, Y.M., Lin, C. Y. 1992. Immunological study of low molecular weight heat shock proteins. Plant Physiol. in presss. 28. Ingolia, T.D., Craig, E.A. 1982. Four amall Drosophila heat shock proteins are related to each other and to mammalian-crystallins. Proc. Natl. Acad. Sci. USA 79:2360-64 29. Ish-Shalom, D., Kloppstech, K., Ohad, I. 1990. Light regulation of the 22 kD heat shock gene transcription and its translation product accumulation in Chlamydomonas reinhardtii. EMBO J. 9:2657-6129. 30. Jinn, T.L., Chen, Y.M., Lin, C.Y. 1989. Stabilization of soluble proteins in vitro by heat shock proteins-enriched ammonium sulfate fraction from soybean seedings. Plant Cell Physiol. 30:463-69 31. Kaksch, W., Mannherz, H.G., Suck, D., Pai, E.F., Holmes K.C. 1990. Atomic structure of the actin: DNase I complex. Nature 347:37-44 32. Kang, P.-J., Ostermenn, J., Schilling, J., Neupert, W., Craig, E. A., et al. 1990. Hsp70 in the mitochondrial matrix is required for translocation and folding of precursor proteins. Nature 348:137-43 33. Kimpel, J.A., Key, J.L. 1985. Heat shock in plants. Trends Biochem. Sci. 10:353-57 34. Kloppstech, K., Meyer, G., Schuster, G., Ohad, I. 1985. Synthesis, transport and localization of a nuclear coded 22kD heat-shock protein in the cholroplast membranes of peas and Chlamydomonas reinhardi. EMBO J. 4:1902-9 35. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-85 36. Leustek, T., Dalie, B., Smir-Shapira, D., Brot, N., Weissbach, H. 1989. A member of the hsp70 family is localized in mitochondria and resembles Escherichia coli DnaK. Proc. Natl. Acad. Sci. USA 86:7805-8 37. Lin, C.-Y., Key, J.L. 1967. Disassociation and reassembly of polyribosomes in relation to protein synthesis in the soybean root. J. Mol. Biol. 26:237-247 38. Lin, C.-Y., Roberts, J.K., Key, J.L. 1984. Acquisition of thermotolerance in soybean seedings. Plant Physiol. 74:152-60 39. Lindquist, S. 1986. The heat shock response. Annu. Rev Biochem. 45:39-72 40. Lindquist, S., Craig, E.A. 1988. The heat shock proteins. Annu. Rev Genet. 22:631-77 41. Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randoll, R.J. 1951. Protein measurement with Folin phenol reagent. J. Biol. Chem. 193:265-275 42. Lubben, T.H., Donaldson, G.K., Viitanen, P.V., Gatenby, A.A. 1989. Several proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperone. Plant Cell 1:1223-30 43. Marshall, J.S., DeRocher, A.E., Keegstra, K., Vierling, E. 1990. Identification of heat shock protein hsp70 homologues in chloroplast. Proc. Natl. Acad. Sci. USA 87: 374-78 44. Minton, K.W., Larmin, P., Hahn, G.M., Minton, A.P. 1982. Non-apecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins. Proc. Natl. Acad. Sci. USA 79:7107-7111 45. Mizzen, L.A., Chang, C., Garrels, J.I., Welch, W.J. 1989. Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp75, a member of the hsp70 family and hsp58, a homolog of the bacterial groEL protein. J. Biol. Chem. 264:20664-75 46. Munro, S., Pelham, H.R.B. 1986. An HSP70-like protein in the ER: identity with the 78kD glucose-regulated pretein and immuniglobulin heavy chain binding protein. Cell 46: 291-300 47. Nagao, R.T., Czarnecka, E., Gurley, W.B., Key, J.L. 1985. Genes for low-molecular-weight heat shock proteins of soybeans: sequence analys is of a multigene family. Mol. Cell. Biol. 5:3417-28 48. Nover, L., Scharf, K.-D., Neumann, D. 1989. Cytoplasmic heat shock granules are formed from precursor particles and are associated with a specific set of mRNAs. Mol. Cell. Biol. 9:1298-308 49. Pelham, H.R.B. 1986. Speculations on the functuons of the major heat shock and glucose regulated proteins. Cell 46: 959-61 50. Pelham, H.R.B. 1989. Control of protein exit from the endoplasmic re ticulum. Annu. Rev. Cell Biol. 5:1-23 51. Petko, L., Lindquist, S. 1986. Hsp26 is not required for growth at high temperatures, not for thermotolerance, spore development or germination. Cell 45:885-94 52. Picard, D., Khursheed, B., Garabedian, M.J., Fortin, M. G., Lindquist, S., Yamamoto, K.R. 1990. Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature 348:166-68 53. Prasad, T.K., Hack, E., Hallberg, R.L. 1990. Function of the maize mitochondrial chaperonin hsp60: specific association between Hsp60 and newly synthesized F1-ATPase alpha sununits. Mol. Cell. Biol. 10:3679-986 54. Prasad, T.K., Hallberg, R.L. 1989. Idintification and metabolic characterization of the Zea mays mitochondiral homolog of the Escherichia coli groEL protein. Plant Mol. Biol. 12:609-18 55. Raschke, E., Baumann, G., Schoffl, F. 1988. Nucleotide sequence analts is of soybean small heat shock genes belonging to two different multigene families. J. Mol. Biol. 199:549-57 56. Rochester, D.E., Winter, J.A., Shah, D.M. 1986. The structure and expression of maize genes encoding the major heat shock protein, hsp70. EMBO J. 5:451-58 57. Romisch, K., Webb, J., Lingelbach, K., Gausepohl, H., D pbberstein, B. 1990. The 54kD protein of signal recognition particle contains a methionine-rich RNA binding domain. J. Cell Biol. 111:1793-1802 58. Rothman, J.E. 1989. Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell 59:591-601 59. Roy, H. 1989. Rubisco assembly: a model system for studying the mechanism of chaperonin action. Plant Cell 1:1035-42 60. Sanchez, Y., Lindquist, S.L. 1990. HSP104 required for induced thermotolerance. Science 248:1112-15 61. Schlesinger, M.J. 1990. Heat shock proteins, J. Biol. Chem. 265:12111-14 62. Skowyra, D., Georgopoulos, C., Zylicz, M. 1990. The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner. Cell 62:939-44 63. Smith, D.B., Johnson, K.S. 1988. Single-step purification of polypeptide expressed in Escherichia coli as fusions with glutathione S-transferase Gene 67:31-40 64. Susek, R.E., Lindquist, S.L. 1989. hsp26 of Saccharomyces cerevisiae is related to the superfamily of small heat shock proteins but is without a demonstrable function. Mol. Cell. Biol. 9:5265-71 65. Vierling E. 1991. The roles of heat shock proteins in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 42:579-620 66. Vierling, E., Nagao, R.T., DeRocher, A.E., Harris, L.M. 1988. A heat shock protein localized to chloroplasts is a member of a erkaryotic superfamily of heat shock proteins. EMBO J. 7:575-81 | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/75884 | - |
| dc.description.abstract | 植物在高溫逆境下會合成大量的低分子量熱休克蛋白質(LMW HSPs),在大豆中,此LMW HSPs 70-100%硫酸銨集濃分劃區內的蛋白質具有熱保護能力,可以使植物可溶性蛋白質在高溫下的變性量降低達50%,此LMW HSPs所保護的對象可能是與膜系統相關的蛋白質,而且沒有任何一種蛋白質受保護的情形較為明顯,不同離子強度對此熱保護作用並無顯著影響。為更進一步證實此熱保護能力來自LMW HSPs,而不是其他HSPs所造成的影響,故直接以純化的水稻LMW HSP融合蛋白質(fusion protein)進行熱保護實驗,結果證實LMW HSP的確能提供熱保護效應,而且熱保護能力會隨著所加入水稻LMW HSP融合蛋白質的增加而增加。除此之外,此熱保護能力在不同植物種類之間具有共通性;另一方面,也對LMW HSPs累積的量與熱保護能力之間的相關性作一探討。 | zh_TW |
| dc.description.abstract | Plants can produce a large amount of Low Molecular Weight heat shock proteins under heat stress. The LMW HSPs enriched 70-100% ammonium-sulphate fraction has the thermoprotection ability to prevent the soluble protein from denaturation under heat stress, and the protection efficiency can reach 50%. The LMW HSPs have the tendency to protect the membrane-related proteins but have no substrate-specificity. Different salt concentration has little effect on this thermoprotection ability. For further confirmation of the thermoprotection ability is mainly from the LMW HSPs, I used the purified rice LMW HSP fusion protein as LMW HSP donator and varified that the LMW HSP solely can contribute the thermoprotection ability to plants. I also found the protection efficiency is proportional to the amount of LMW HSPs added. Besides these, the thermoprotection ability is changeable among different kind of plants. On the other hand, I have tried to find out the relationship between the amount of LMW HSPs accumulation and the thermoprotection ability. | en |
| dc.description.provenance | Made available in DSpace on 2021-07-01T08:16:10Z (GMT). No. of bitstreams: 0 Previous issue date: 1992 | en |
| dc.description.tableofcontents | 中文摘要……………………………………………………1 英文摘要……………………………………………………2 前言……………………………………………………3 材料與方法……………………………………………………15 結果……………………………………………………27 討論……………………………………………………48 參考文獻……………………………………………………54 | |
| dc.language.iso | zh-TW | |
| dc.title | 植物低分子量熱休克蛋白質的生理功能 | zh_TW |
| dc.title | The Biological Function of Low Molecular Weight Heat Shock Proteins in Plants | en |
| dc.date.schoolyear | 80-2 | |
| dc.description.degree | 碩士 | |
| dc.relation.page | 61 | |
| dc.rights.note | 未授權 | |
| dc.contributor.author-dept | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 植物科學研究所 | zh_TW |
| 顯示於系所單位: | 植物科學研究所 | |
文件中的檔案:
沒有與此文件相關的檔案。
系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。
