Skip navigation

DSpace

機構典藏 DSpace 系統致力於保存各式數位資料(如:文字、圖片、PDF)並使其易於取用。

點此認識 DSpace
DSpace logo
English
中文
  • 瀏覽論文
    • 校院系所
    • 出版年
    • 作者
    • 標題
    • 關鍵字
    • 指導教授
  • 搜尋 TDR
  • 授權 Q&A
    • 我的頁面
    • 接受 E-mail 通知
    • 編輯個人資料
  1. NTU Theses and Dissertations Repository
  2. 醫學院
  3. 微生物學科所
請用此 Handle URI 來引用此文件: http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/60477
完整後設資料紀錄
DC 欄位值語言
dc.contributor.advisor李財坤(Tsai-Kun Li)
dc.contributor.authorChih-Yao Liuen
dc.contributor.author劉至堯zh_TW
dc.date.accessioned2021-06-16T10:19:14Z-
dc.date.available2018-09-24
dc.date.copyright2013-09-24
dc.date.issued2013
dc.date.submitted2013-08-16
dc.identifier.citationREFERENCES
Aguilera, A., and Garcia-Muse, T. (2012). R loops: from transcription byproducts to threats to genome stability. Molecular cell 46, 115-124.
Aldridge, M., Facey, P., Francis, L., Bayliss, S., Del Sol, R., and Dyson, P. (2013). A novel bifunctional histone protein in Streptomyces: a candidate for structural coupling between DNA conformation and transcription during development and stress? Nucleic acids research 41, 4813-4824.
Azam, T.A., Hiraga, S., and Ishihama, A. (2000). Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid. Genes to cells : devoted to molecular & cellular mechanisms 5, 613-626.
Azam, T.A., and Ishihama, A. (1999). Twelve species of the nucleoid-associated protein from Escherichia coli. Sequence recognition specificity and DNA binding affinity. The Journal of biological chemistry 274, 33105-33113.
Azam, T.A., Iwata, A., Nishimura, A., Ueda, S., and Ishihama, A. (1999a). Growth phase-dependent variation in protein composition of the escherichia coli nucleoid. Journal of bacteriology 181, 6361-6379.
Azam, T.A., Iwata, A., Nishimura, A., Ueda, S., and Ishihama, A. (1999b). Growth phase-dependent variation in protein composition of the escherichia coli nucleoid. Journal of bacteriology 181, 6361-6370.
Baba, T., Ara, T., Hasegawa, M., Takai, Y., Okumura, Y., Baba, M., Datsenko, K.A., Tomita, M., Wanner, B.L., and Mori, H. (2006). Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2, 2006 0008.
Balandina, A., Kamashev, D., and Rouviere-Yaniv, J. (2002). The bacterial histone-like protein HU specifically recognizes similar structures in all nucleic acids. DNA, RNA, and their hybrids. The Journal of biological chemistry 277, 27622-27628.
Baldacci, G., Cherif-Zahar, B., and Bernardi, G. (1984). The initiation of DNA replication in the mitochondrial genome of yeast. Embo J 3, 2115-2120.
Becker, N.A., Kahn, J.D., and Maher, L.J., 3rd (2007). Effects of nucleoid proteins on DNA repression loop formation in Escherichia coli. Nucleic acids research 35, 3988-4000.
Belotserkovskii, B.P., Neil, A.J., Saleh, S.S., Shin, J.H., Mirkin, S.M., and Hanawalt, P.C. (2013). Transcription blockage by homopurine DNA sequences: role of sequence composition and single-strand breaks. Nucleic acids research 41, 1817-1828.
Berger, M., Farcas, A., Geertz, M., Zhelyazkova, P., Brix, K., Travers, A., and Muskhelishvili, G. (2010). Coordination of genomic structure and transcription by the main bacterial nucleoid-associated protein HU. EMBO reports 11, 59-64.
Bonnefoy, E., Takahashi, M., and Yaniv, J.R. (1994). DNA-binding parameters of the HU protein of Escherichia coli to cruciform DNA. J Mol Biol 242, 116-129.
Boubakri, H., de Septenville, A.L., Viguera, E., and Michel, B. (2010). The helicases DinG, Rep and UvrD cooperate to promote replication across transcription units in vivo. Embo J 29, 145-157.
Bransteitter, R., Pham, P., Scharff, M.D., and Goodman, M.F. (2003). Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. Proceedings of the National Academy of Sciences of the United States of America 100, 4102-4107.
Broyles, S.S., and Pettijohn, D.E. (1986). Interaction of the Escherichia coli HU protein with DNA. Evidence for formation of nucleosome-like structures with altered DNA helical pitch. J Mol Biol 187, 47-60.
Bushnell, D.A., Cramer, P., and Kornberg, R.D. (2002). Structural basis of transcription: alpha-amanitin-RNA polymerase II cocrystal at 2.8 A resolution. Proceedings of the National Academy of Sciences of the United States of America 99, 1218-1222.
Cardinale, C.J., Washburn, R.S., Tadigotla, V.R., Brown, L.M., Gottesman, M.E., and Nudler, E. (2008). Termination factor Rho and its cofactors NusA and NusG silence foreign DNA in E. coli. Science 320, 935-938.
Castaing, B., Zelwer, C., Laval, J., and Boiteux, S. (1995). Hu protein of Escherichia coli binds specifically to DNA that contains single-strand breaks or gaps. The Journal of biological chemistry 270, 10291-10296.
Claverie-Martin, F., and Magasanik, B. (1992). Positive and negative effects of DNA bending on activation of transcription from a distant site. J Mol Biol 227, 996-1008.
Dame, R.T. (2005). The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin. Molecular microbiology 56, 858-870.
Deng, S., Stein, R.A., and Higgins, N.P. (2005). Organization of supercoil domains and their reorganization by transcription. Molecular microbiology 57, 1511-1521.
Dillon, S.C., and Dorman, C.J. (2010). Bacterial nucleoid-associated proteins, nucleoid structure and gene expression. Nature reviews Microbiology 8, 185-195.
Dorman, C.J. (2004). H-NS: a universal regulator for a dynamic genome. Nature reviews Microbiology 2, 391-400.
Dorman, C.J. (2013). Co-operative roles for DNA supercoiling and nucleoid-associated proteins in the regulation of bacterial transcription. Biochemical Society transactions 41, 542-547.
Drlica, K., and Rouviere-Yaniv, J. (1987). Histonelike proteins of bacteria. Microbiol Rev 51, 301-319.
Drolet, M., Phoenix, P., Menzel, R., Masse, E., Liu, L.F., and Crouch, R.J. (1995). Overexpression of RNase H partially complements the growth defect of an Escherichia coli deltatopA mutant R-loop formation is a major problem in the absence of DNA topoisomerase I. Proceedings of the National Academy of Sciences of the United States of America 92, 3526-3530.
Dudas, K.C., and Kreuzer, K.N. (2001). UvsW protein regulates bacteriophage T4 origin-dependent replication by unwinding R-loops. Molecular and cellular biology 21, 2706-2715.
Duquette, M.L., Handa, P., Vincent, J.A., Taylor, A.F., and Maizels, N. (2004). Intracellular transcription of G-rich DNAs induces formation of G-loops, novel structures containing G4 DNA. Genes Dev 18, 1618-1629.
Dworsky, P., and Schaechter, M. (1973). Effect of rifampin on the structure and membrane attachment of the nucleoid of Escherichia coli. Journal of bacteriology 116, 1364-1374.
El Hage, A., French, S.L., Beyer, A.L., and Tollervey, D. (2010). Loss of Topoisomerase I leads to R-loop-mediated transcriptional blocks during ribosomal RNA synthesis. Genes Dev 24, 1546-1558.
French, S.L., Sikes, M.L., Hontz, R.D., Osheim, Y.N., Lambert, T.E., El Hage, A., Smith, M.M., Tollervey, D., Smith, J.S., and Beyer, A.L. (2011). Distinguishing the roles of Topoisomerases I and II in relief of transcription-induced torsional stress in yeast rRNA genes. Molecular and cellular biology 31, 482-494.
Gan, W., Guan, Z., Liu, J., Gui, T., Shen, K., Manley, J.L., and Li, X. (2011). R-loop-mediated genomic instability is caused by impairment of replication fork progression. Genes Dev 25, 2041-2056.
Ginno, P.A., Lott, P.L., Christensen, H.C., Korf, I., and Chedin, F. (2012). R-loop formation is a distinctive characteristic of unmethylated human CpG island promoters. Molecular cell 45, 814-825.
Goosen, N., and van de Putte, P. (1995). The regulation of transcription initiation by integration host factor. Molecular microbiology 16, 1-7.
Grabczyk, E., Mancuso, M., and Sammarco, M.C. (2007). A persistent RNA.DNA hybrid formed by transcription of the Friedreich ataxia triplet repeat in live bacteria, and by T7 RNAP in vitro. Nucleic acids research 35, 5351-5359.
Grainger, D.C., Goldberg, M.D., Lee, D.J., and Busby, S.J. (2008). Selective repression by Fis and H-NS at the Escherichia coli dps promoter. Molecular microbiology 68, 1366-1377.
Grainger, D.C., Hurd, D., Goldberg, M.D., and Busby, S.J. (2006). Association of nucleoid proteins with coding and non-coding segments of the Escherichia coli genome. Nucleic acids research 34, 4642-4652.
Hardy, C.D., and Cozzarelli, N.R. (2005). A genetic selection for supercoiling mutants of Escherichia coli reveals proteins implicated in chromosome structure. Molecular microbiology 57, 1636-1652.
Higgins, N.P. (2005). The bacterial chromosome (Washington, DC: American Society for Microbiology).
Hong, X., Cadwell, G.W., and Kogoma, T. (1995). Escherichia coli RecG and RecA proteins in R-loop formation. Embo J 14, 2385-2392.
Huang, F.T., Yu, K., Hsieh, C.L., and Lieber, M.R. (2006). Downstream boundary of chromosomal R-loops at murine switch regions: implications for the mechanism of class switch recombination. Proceedings of the National Academy of Sciences of the United States of America 103, 5030-5035.
Huang, S.-Y. (2006). Regulation of R-loop formation and its implications: AID-stimulated mutagenesis. In Department and Graduate Institute of Microbiology (National Taiwan University).
Huertas, P., and Aguilera, A. (2003). Cotranscriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination. Molecular cell 12, 711-721.
Huo, Y.X., Zhang, Y.T., Xiao, Y., Zhang, X., Buck, M., Kolb, A., and Wang, Y.P. (2009). IHF-binding sites inhibit DNA loop formation and transcription initiation. Nucleic acids research 37, 3878-3886.
Itoh, T., and Tomizawa, J.-I. (1980). Formation of an RNA primer for initiation of replication of ColE1 DNA by ribonuclease H. Proceedings of the National Academy of Sciences of the United States of America 77, 2450-2454.
Johnson, S.E.F.a.R.C. (1992). The Fis protein it's not just for DNA inversion anymore. Molecular microbiology 6, 3257-3265.
Justive, S.S., Hunstad, D.A., Cegelski, L., and Hultgren, S.J. (2008). Morphological plasticity as bacterial survival strategy. Nature reviews Microbiology 6, 162-168.
Kadesch, T.R., and Chamberlin, M.J. (1982). Studies of in vitro transcription by calf thymus RNA polymerase II using a novel duplex DNA template. The Journal of biological chemistry 257, 5286-5295.
Kajitani, M., Kato, A., Wada, A., Inokuchi, Y., and Ishihama, A. (1994). Regulation of the Escherichia coli hfq gene encoding the host factor for phage Q beta. Journal of bacteriology 176, 531-534.
Kamashev, D., Balandina, A., Mazur, A.K., Arimondo, P.B., and Rouviere-Yaniv, J. (2008). HU binds and folds single-stranded DNA. Nucleic acids research 36, 1026-1036.
Kamashev, D., Balandina, A., and Rouviere-Yaniv, J. (1999). The binding motif recognized by HU on both nicked and cruciform DNA. Embo J 18, 5434-5444.
Kamashev, D., and Rouviere-Yaniv, J. (2000). The histone-like protein HU binds specifically to DNA recombination and repair intermediates. Embo J 19, 6527-6535.
Kano, Y., and Imamoto, F. (1990). Requirment of integration host factor for growth of Escherichia coli deficient in HU protein. Gene 89, 133-137.
Kao, Y.P., Hsieh, W.C., Hung, S.T., Huang, C.W., Lieber, M.R., and Huang, F.T. (2013). Detection and characterization of R-loops at the murine immunoglobulin Salpha region. Molecular immunology 54, 208-216.
Kasahara, M., Clikeman, J.A., Bates, D.B., and Kogoma, T. (2000). RecA protein-dependent R-loop formation in vitro. Genes Dev 14, 360-365.
Kavenoff, R., and Bowen, B.C. (1976). Eletron microscopy of membrane-free folded chromosomes from Escherichia coli. Chromosome, 89-101.
Kim, J., Yoshimura, S.H., Hizume, K., Ohniwa, R.L., Ishihama, A., and Takeyasu, K. (2004). Fundamental structural units of the Escherichia coli nucleoid revealed by atomic force microscopy. Nucleic acids research 32, 1982-1992.
Kim, N., and Jinks-Robertson, S. (2011). Guanine repeat-containing sequences confer transcription-dependent instability in an orientation-specific manner in yeast. DNA repair 10, 953-960.
Kobryn, K., Lavoie, B.D., and Chaconas, G. (1999). Supercoiling-dependent site-specific binding of HU to naked Mu DNA. J Mol Biol 289, 777-784.
Leela, J.K., Syeda, A.H., Anupama, K., and Gowrischankar, J. (2012). Rho-dependent transcription termination is essential to prevent excessibe genome-wide R-loops in Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America 110, 258-263.
Li, X., and Manley, J.L. (2005). Inactivation of the SR protein splicing factor ASF/SF2 results in genomic instability. Cell 122, 365-378.
Li, X., and Manley, J.L. (2006). Cotranscriptional processes and their influence on genome stability. Genes Dev 20, 1838-1847.
Lin, Y., Dent, S.Y., Wilson, J.H., Wells, R.D., and Napierala, M. (2010). R loops stimulate genetic instability of CTG.CAG repeats. Proceedings of the National Academy of Sciences of the United States of America 107, 692-697.
Liu, L.F., and Wang, J.C. (1987). Supercoiling of the DNA template during transcription. Proceedings of the National Academy of Sciences of the United States of America 84, 7024-7027.
Malik, M., Bensaid, A., Rouviere-Yaniv, J., and Drlica, K. (1996). Histone-like protein HU and bacterial DNA topology: suppression of an HU deficiency by gyrase mutations. J Mol Biol 256, 66-76.
Marc Drolet, X.B., and Leroy F. Liu (1994). Hypernegative supercoiling of the DNA template during transcription elongation in vitro. The Journal of biological chemistry 269, 2068-2074.
Masse, E., and Drolet, M. (1999). Escherichia coli DNA topoisomerase I inhibits R-loop formation by relaxing transcription-induced negative supercoiling. The Journal of biological chemistry 274, 16659-16664.
Masse, E., Phoenix, P., and Drolet, M. (1997). DNA topoisomerases regulate R-loop formation during transcription of the rrnB operon in Escherichia coli. The Journal of biological chemistry 272, 12816-12823.
McLeod, S.M., and Johnson, R.C. (2001). Control of transcription by nucleoid proteins. Curr Opin Microbiol 4, 152-159.
Meyenburg, K.v., Boye, E., Skarstad, K., Koppes, L., and Kogoma, T. (1987). Mode of initiation of constitutive stable DNA replication in RNase H-defective mutants of Escherichia coli K-12. Journal of bacteriology 169, 2650-2658.
Mischo, H.E., Gomez-Gonzalez, B., Grzechnik, P., Rondon, A.G., Wei, W., Steinmetz, L., Aguilera, A., and Proudfoot, N.J. (2011). Yeast Sen1 helicase protects the genome from transcription-associated instability. Molecular cell 41, 21-32.
Mizuta, R., Iwai, K., Shigeno, M., Mizuta, M., Uemura, T., Ushiki, T., and Kitamura, D. (2003). Molecular visualization of immunoglobulin switch region RNA/DNA complex by atomic force microscope. The Journal of biological chemistry 278, 4431-4434.
Morales, P., Rouviere-Yaniv, J., and Dreyfus, M. (2002). The Histone-Like Protein HU Does Not Obstruct Movement of T7 RNA Polymerase in Escherichia coli Cells but Stimulates Its Activity. Journal of bacteriology 184, 1565-1570.
Muramatsu, M., Kinoshita, K., Fagarasan, S., Yamada, S., Shinkai, Y., and Honjo, T. (2000). Class switch recombination and hypermutation require activation-induce cytidine deaminase (AID), a potential RNA editing enzyme. Cell 102.
Nonaka, S., Shiratori, H., Saijoh, Y., and Hamada, H. (2002). Determination of left-right patterning of the mouse embryo by artificial nodal flow. Nature 418, 96-99.
Noom, M.C., Navarre, W.W., Oshima, T., Wuite, G.J., and Dame, R.T. (2007). H-NS promotes looped domain formation in the bacterial chromosome. Current biology : CB 17, R913-914.
Ohniwa, R.L., Morikawa, K., Kim, J., Ohta, T., Ishihama, A., Wada, C., and Takeyasu, K. (2006). Dynamic state of DNA topology is essential for genome condensation in bacteria. Embo J 25, 5591-5602.
Ohniwa, R.L., Morikawa, K., Takeshita, S.L., Kim, J., Ohta, T., Wada, C., and Takeyasu, K. (2007). Transcription-coupled nucleoid architecture in bacteria. Genes to cells : devoted to molecular & cellular mechanisms 12, 1141-1152.
Ohniwa, R.L., Ushijima, Y., Saito, S., and Morikawa, K. (2011). Proteomic analyses of nucleoid-associated proteins in Escherichia coli, Pseudomonas aeruginosa, Bacillus subtilis, and Staphylococcus aureus. PLoS One 6, e19172.
Paulsen, R.D., Soni, D.V., Wollman, R., Hahn, A.T., Yee, M.C., Guan, A., Hesley, J.A., Miller, S.C., Cromwell, E.F., Solow-Cordero, D.E., et al. (2009). A genome-wide siRNA screen reveals diverse cellular processes and pathways that mediate genome stability. Molecular cell 35, 228-239.
Petersen-Mahrt, S.K., Harris, E.S., and Neuberger, M.S. (2002). AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification. Nature 418, 99-103.
Pham, P., Bransteitter, R., Petruska, J., and Goodman, M.F. (2003). Processive AID-catalysed cytosine deamination on single-stranded DNA simulates somatic hypermutation. Nature 424, 103-107.
Pomerantz, R.T., and O'Donnell, M. (2008). The replisome uses mRNA as a primer after colliding with RNA polymerase. Nature 456, 762-766.
Pontiggia, A., Negri, A., Beltrame, M., and Bianchi, M.E. (1993). Protein HU binds specifically to kinked DNA. Molecular microbiology 7, 343-350.
Postow, L., Hardy, C.D., Arsuaga, J., and Cozzarelli, N.R. (2004). Topological domain structure of the Escherichia coli chromosome. Genes Dev 18, 1766-1779.
Ramiro, A.R., Stavropoulos, P., Jankovic, M., and Nussenzweig, M.C. (2003). Transcription enhances AID-mediated cytidine deamination by exposing single-stranded DNA on the nontemplate strand. Nature immunology 4, 452-456.
Reddy, K., Tam, M., Bowater, R.P., Barber, M., Tomlinson, M., Nichol Edamura, K., Wang, Y.H., and Pearson, C.E. (2011). Determinants of R-loop formation at convergent bidirectionally transcribed trinucleotide repeats. Nucleic acids research 39, 1749-1762.
Rindler, P.M., and Bidichandani, S.I. (2011). Role of transcript and interplay between transcription and replication in triplet-repeat instability in mammalian cells. Nucleic acids research 39, 526-535.
Roberts, R.W., and Crothers, D.M. (1992). Stability and properties of double and triple helices - dramatic effects of RNA or DNA backbone composition. Science 258, 1463-1466.
Rouviere-Yaniv, J., and Yaniv, M. (1979). E. coli DNA binding protein HU forms nucleosome-like structure with circular double-stranded DNA. Cell 17, 265-274.
Roy, D., and Lieber, M.R. (2009). G clustering is important for the initiation of transcription-induced R-loops in vitro, whereas high G density without clustering is sufficient thereafter. Molecular and cellular biology 29, 3124-3133.
Roy, D., Yu, K., and Lieber, M.R. (2008). Mechanism of R-loop formation at immunoglobulin class switch sequences. Molecular and cellular biology 28, 50-60.
Roy, D., Zhang, Z., Lu, Z., Hsieh, C.L., and Lieber, M.R. (2010). Competition between the RNA transcript and the nontemplate DNA strand during R-loop formation in vitro: a nick can serve as a strong R-loop initiation site. Molecular and cellular biology 30, 146-159.
Saxena, S., and Gowrishankar, J. (2011). Modulation of Rho-dependent transcription termination in Escherichia coli by the H-NS family of proteins. Journal of bacteriology 193, 3832-3841.
Schneider, R., Travers, A., Kutateladze, T., and Muskhelishvili, G. (1999). A DNA architectural protein couples cellular physiology and DNA topology in Escherichia coli. Molecular microbiology 34, 953-964.
Shi, X., and Bennett, G.N. (1994). Plasmids bearing hfq and the hns-like gene stpA complement hns mutants in modulating arginine decarboxylase gene expression in Escherichia coli. Journal of bacteriology 176, 6769-6775.
Shinkura, R., Tian, M., Smith, M., Chua, K., Fujiwara, Y., and Alt, F.W. (2003). The influence of transcriptional orientation on endogenous switch region function. Nature immunology 4, 435-441.
Sikdar, N., Banerjee, S., Zhang, H., Smith, S., and Myung, K. (2008). Spt2p defines a new transcription-dependent gross chromosomal rearrangement pathway. PLoS genetics 4, e1000290.
Silberstein, Z., and Cohen, A. (1987). Synthesis of linear multimers of OriC and pBR322 derivatives in Escherichia coli K-12: role of recombination and replication functions. Journal of bacteriology 169, 3131-3137.
Stirling, P.C., Chan, Y.A., Minaker, S.W., Aristizabal, M.J., Barrett, I., Sipahimalani, P., Kobor, M.S., and Hieter, P. (2012). R-loop-mediated genome instability in mRNA cleavage and polyadenylation mutants. Genes Dev 26, 163-175.
Sugimoto, N., Nakano, S., Katoh, M., Matsumura, A., Nakamuta, H., Ohmichi, T., Yoneyama, M., and Sasaki, M. (1995). Thermodynamic parameters to predict stability of RNA/DNA hybrid duplexes. Biochemistry 34, 11211-11216.
Sun, Q., Csorba, T., Skourti-Stathaki, K., Proudfoot, N.J., and Dean, C. (2013). R-loop stabilization represses antisense transcription at the Arabidopsis FLC locus. Science 340, 619-621.
Swiercz, J.P., Nanji, T., Gloyd, M., Guarne, A., and Elliot, M.A. (2013). A novel nucleoid-associated protein specific to the actinobacteria. Nucleic acids research 41, 4171-4184.
Takada, A., Wachi, M., Kaidow, A., Takamura, M., and Nagai, K. (1997). DNA binding properties of the hfq gene product of Escherichia coli. Biochem Biophys Res Commun 236, 576-579.
Tanaka, H., Yasuzawa, K., Kohno, K., Goshima, N., Kano, Y., Saiki, T., and Imamoto, F. (1995). Role of HU proteins in forming and constraining supercoils of chromosomal DNA in Escherichia coli. Mol Gen Genet 248, 518-526.
Thomas, M., White, R.L., and Davis, R.W. (1976). Hybridication of RNA to double-stranded DNA formation of R-loops. Proceedings of the National Academy of Sciences of the United States of America 73, 2294-2298.
Tian, M., and Alt, F.W. (2000). Transcription-induced cleavage of immunoglobulin switch regions by nucleotide excision repair nucleases in vitro. The Journal of biological chemistry 275, 24163-24172.
Tran, L., van Baarsel, J.A., Washburn, R.S., Gottesman, M.E., and Miller, J.H. (2011). Single-gene deletion mutants of Escherichia coli with altered sensitivity to bicyclomycin, an inhibitor of transcription termination factor Rho. Journal of bacteriology 193, 2229-2235.
Tuduri, S., Crabbe, L., Conti, C., Tourriere, H., Holtgreve-Grez, H., Jauch, A., Pantesco, V., De Vos, J., Thomas, A., Theillet, C., et al. (2009). Topoisomerase I suppresses genomic instability by preventing interference between replication and transcription. Nature cell biology 11, 1315-1324.
Tupper, A.E., Owen-Hughes, T.A., Ussery, D.W., Santos, D.S., Ferguson, D.J.P., Siderbotham, J.M., Hinton, J.C.D., and Higgins, C.F. (1994). The chromatin-associated protein H-NS alters DNA topology in vitro. Embo J 13, 258-268.
Ueda, T., Takahashi, H., Uyar, E., Ishikawa, S., Ogasawara, N., and Oshima, T. (2013). Functions of the Hha and YdgT Proteins in Transcriptional Silencing by the Nucleoid Proteins, H-NS and StpA, in Escherichia coli. DNA research : an international journal for rapid publication of reports on genes and genomes 20, 263-271.
Updegrove, T.B., Correia, J.J., Galletto, R., Bujalowski, W., and Wartell, R.M. (2010). E. coli DNA associated with isolated Hfq interacts with Hfq's distal surface and C-terminal domain. Biochimica et biophysica acta 1799, 588-596.
Vogel, J., and Luisi, B.F. (2011). Hfq and its constellation of RNA. Nature reviews Microbiology 9, 578-589.
Wada, M., Kano, Y., Ogawa, T., Okazaki, T., and Imamoto, F. (1988). Construction and characterization of the deletion mutant of hupA and hupB genes in Escherichia coli. J Mol Biol 204, 581-591.
Wahba, L., Amon, J.D., Koshland, D., and Vuica-Ross, M. (2011). RNase H and multiple RNA biogenesis factors cooperate to prevent RNA:DNA hybrids from generating genome instability. Molecular cell 44, 978-988.
Wahba, L., Gore, S.K., and Koshland, D. (2013). The homologous recombination machinery modulates the formation of RNA-DNA hybrids and associated chromosome instability. eLIFE 2, e00505.
Wanrooij, P.H., Uhler, J.P., Shi, Y., Westerlund, F., Falkenberg, M., and Gustafsson, C.M. (2012). A hybrid G-quadruplex structure formed between RNA and DNA explains the extraordinary stability of the mitochondrial R-loop. Nucleic acids research 40, 10334-10344.
Washburn, R.S., and Gottesman, M.E. (2011). Transcription termination maintains chromosome integrity. Proceedings of the National Academy of Sciences of the United States of America 108, 792-797.
Watkins, N.E., Jr., Kennelly, W.J., Tsay, M.J., Tuin, A., Swenson, L., Lee, H.R., Morosyuk, S., Hicks, D.A., and Santalucia, J., Jr. (2011). Thermodynamic contributions of single internal rA.dA, rC.dC, rG.dG and rU.dT mismatches in RNA/DNA duplexes. Nucleic acids research 39, 1894-1902.
Weinstein-Fischer, D., and Altuvia, S. (2007). Differential regulation of Escherichia coli topoisomerase I by Fis. Molecular microbiology 63, 1131-1144.
Weinstein-Fischer, D., Elgrably-Weiss, M., and Altuvia, S. (2000). Escherichia coli response to hydrogen peroxide: a role for DNA supercoiling, topoisomerase I and Fis. Molecular microbiology 35, 1413-1420.
Wen, C.-Y. (2009). Regulation and biological functions of R-loop: Roles of RecF pathway and DNA topoisomerases. In Department and Graduate Institute of Microbiology (National Taiwan University).
White, R.L., and Hogness, D.S. (1977). R loop mapping of the 18S and 28S sequences in the long and short repeating units of Drosophila melanogaster rDNA. Cell 10, 177-192.
Woldringh, C.L., Jensen, P.R., and Westerhoff, H.V. (1995). Structure and partitioning of bacterial DNA: determined by a balance of compaction and expansion forces? FEMS Microbiol Lett 131, 235-242.
Wongsurawat, T., Jenjaroenpun, P., Kwoh, C.K., and Kuznetsov, V. (2012). Quantitative model of R-loop forming structures reveals a novel level of RNA-DNA interactome complexity. Nucleic acids research 40, e16.
Woroel, A., and Burgi, E. (1972). On the structure of the folded chromosome of Escherichia coli. J Mol Biol, 127-147.
Yasuzawa, K., Hayashi, N., Goshima, N., Kohno, K., Imamoto, F., and Kano, Y. (1992). Histone-like proteins are required for cell growth and constraint of supercoils in DNA. Gene 122, 9-15.
Yu, K., Chedin, F., Hsieh, C.L., Wilson, T.E., and Lieber, M.R. (2003). R-loops at immunoglobulin class switch regions in the chromosomes of stimulated B cells. Nature immunology 4, 442-451.
Zaitsev, E.N., and Kowalczykowski, S.C. (2000). A novel pairing process promoted by Escherichia coli RecA protein: inverse DNA and RNA strand exchange. Genes Dev 14, 740-749.
Zulianello, L., Derosny, E.D., Vanulsen, P., Vandeputte, P., and Goosen, N. (1994). The HimA and HimD subunits of integration host factor can specifically bind to DNA as homodimers. Embo J 13, 1534-1540.
dc.identifier.urihttp://tdr.lib.ntu.edu.tw/jspui/handle/123456789/60477-
dc.description.abstract中文摘要
R-loop是一種雙股去氧核糖核酸(DNA)被新生成的核糖核酸侵入所形成的結構,偶爾會在轉錄延伸的過程中發生。這種結構參與在許多生物的作用之中,例如ColE1質體的複製起始(initiation of ColE1 plasmid DNA replication)、免疫球蛋白體細胞超突變和類型轉換重組(immunoglobulin somatic hypermutation and class switch recombination)及表觀基因調控(epigenetic regulation)等。然而,前人的研究發現R-loop的形成會導致複製叉(replication fork)停滯、轉錄障礙以及基因組不穩定,因此,細胞中具有許多因子會調控R-loop的形成,使其達到動態平衡。不過對於R-loop調控的機制卻仍舊有許多未知的地方。我們利用活化誘導胞嘧啶核苷脫氨酶(Activation-induced cytidine deaminase, AID)來偵測大腸桿菌模式系統中R-loop的形成。AID可作用在R-loop中的單股DNA,將上面的胞嘧啶(cytosine)脫氨化轉變成尿嘧啶(uracil),因而產生致突變性(mutagenesis)。因此從AID刺激突變機率所計算而得到的倍數(AID-stimulated mutagenesis fold, ASM fold)可用來表示胞內R-loop的多寡。透過這個實驗模式系統,進一步證明DNA拓樸異構酶(DNA topoisomerases)會在核糖核酸聚合酶(RNA polymerase)的前後端維持DNA超螺旋(DNA supercoiling)的結構,我們發現細菌第一型拓樸酶TopA可負向調控R-loop的形成,而第二型拓樸酶gyrase可正向調控R-loop的形成,這也。基於以上發現,我們假設R-loop可以被一群有能力改變DNA拓樸結構的因子所調控,例如DNA拓樸異構酶或是與類核體結合之相關結構蛋白等。在本篇論文中,我們想發掘在大腸桿菌中主要的類核體相關蛋白(nucleoid-associated proteins, NAPs),其中包含Fis、Hfq、H-NS、StpA、IHF及HU蛋白,在R-loop的調控中所扮演的角色。首先,我們確定在不同NAPs突變株中,質體DNA的拓樸結構的確會受到影響。接下來我們發現IHF可逆向調控R-loop形成,其基因去除可造成較野生型高的ASM倍數、較多的Sγ3表達質體所造成的死亡(Sγ3 plasmid-mediated lethality)以及細菌之細胞延長(cellular elongation)。相反地,HU可正向調控R-loop形成,其基因去除可造成較低的ASM fold、較少的Sγ3質體所造成的死亡以及沒有細胞延長。因此,我們首先發現參與在組成類核體結構中的因子同時可以調控R-loop的形成。我們的研究提供了第一次實驗證據這些類核體相關蛋白因子不只在類核體結構上扮演角色,更可以進一步影響DNA複製起始、轉錄相關重組(transcription-associated recombination)以及基因不穩定性等生物作用。
關鍵詞:類核體;類核體相關蛋白;轉錄;R-loop;活化誘導胞嘧啶核苷脫氨酶;DNA拓樸異構酶;基因不穩定性
zh_TW
dc.description.abstractABSTRACT
R-loop is a structure of double-stranded DNA invaded by nascent RNA, which forms during transcription elongation occasionally. It has been suggested to play roles in the various biological processes such as the initiation of ColE1 plasmid DNA replication, immunoglobulin class switch recombination and epigenetic regulation. In addition, previous studies have also suggested that excess R-loop could result in replication fork stall, transcription blockage and genome instability. Thus, cells have developed many cellular factors to regulate R-loop formation in a low-level homeostasis. Nevertheless, the underlying mechanisms of the regulation of R-loop remain largely unsolved. We have utilized the mutagenic activity of AID to detect R-loop formation in an E. coli model system. AID deaminates cytosine converting it into uracil on the single-stranded DNA in R-loop and the rendering mutagenesis. Therefore, the mutation fold calculated from AID-stimulated mutagenesis assay (ASM fold) is suggestive of the intracellular level of R-loop. Through this system, we have provided experimental supports for the previous “twin-supercoiling domain” hypothesis that topoisomerases maintain the steady state of DNA supercoiling ahead of and behind transcription machinery and identified type I topoisomerase TopA as a suppressive factor for R-loop formation and type II topoisomerase gyrase as a promoting factor for R-loop formation. Based on above discoveries, we have hypothesized that factors involved in changing the topology and structure of DNA may participate in the regulation of R-loop formation, such as DNA topoisomerase and the nucleoid-associated proteins (NAPs). In this study, we further explored the potential roles of major nucleoid-associated proteins in E. coli, including Fis, Hfq, H-NS, StpA, IHF and HU, in regulating R-loop formation, possibly through altering and maintaining the topology and organization of nucleoid DNA. We have confirmed that the topological state of a reporter plasmid was affected differentially in NAP-deleted strains, suggesting their ability to alter the DNA topology and possibly structure. Using the experimental systems for indicating R-loop formation, we have then identified IHF as a potential negative regulator of R-loop formation, whose gene deletion resulted in higher ASM fold, more Sγ3 plasmid-mediated lethality and bacterial cells to elongation (cellular filamentation). In contrast, HU serves as a potential positive regulator of R-loop formation, whose gene deletion led to lower ASM fold, reduced Sγ3 plasmid-mediated lethality and no cellular filamentation. Hence, for the first time, our results revealed that factors involved in organization of nucleoid DNA, participate in regulation of R-loop formation. Subsequently, through regulating R-loop formation, these factors might then contribute to initiation of DNA replication, transcription-associated recombination, and genome instability.
Key words: Nucleoid; Nucleoid-associated proteins; Transcription; R-loop; Activation-induced cytidine deaminase (AID); DNA topoisomerases; Genome instability
en
dc.description.provenanceMade available in DSpace on 2021-06-16T10:19:14Z (GMT). No. of bitstreams: 1
ntu-102-R00445131-1.pdf: 18918807 bytes, checksum: c2920e1e7cc219e9d2eb47ced426b56a (MD5)
Previous issue date: 2013
en
dc.description.tableofcontentsTABLE OF CONTENTS
目錄
中文摘要 i
ABSTRACT iii
INTRODUCTION 1
1 R-loop 1
1.1 Formation of R-loop 1
1.1.1 Two proposed models of R-loop formation 2
1.1.2 Characteristics of R-loop 3
1.2 Biological functions of R-loop 3
1.2.1 The Initiation of DNA replication in B cell 4
1.2.2 AID-mediated antibody diversification 4
1.2.3 Other R-loop-mediated biological functions 5
1.3 Regulation of R-loop 6
1.3.1 DNA sequence, topology and organization 6
1.3.2 Regulation of R-loop by nuclease degradation 8
1.3.3 Co-transcriptional processes during transcription elongation 9
1.3.4 Transcription termination and R-loop regulation by RNA helicases 10
1.3.5 Other mechanisms involved in the regulation of R-loop formation 10
2 Nucleoid-associated proteins (NAPs) 12
2.1 Nucleoid structure 13
2.2 NAPs and nucleoid structure 13
2.3 NAPs and DNA supercoiling 15
2.4 NAPs and transcription 15
SPECIFIC AIMS 17
MATERIALS AND METHODS 18
Escherichia coli strains and plasmids 18
Media and growth conditions 18
Preparation of competent cells 19
Transformation 19
AID-stimulated mutagenesis (ASM) assay 19
Determination of efficiency of plating (EoP) 20
Fluorescence microscopy for cellular filamentation assay 21
Supercoiling assay and measurement 21
Statistic analysis 22
RESULTS 23
Different nucleoid-associated proteins displayed differential superhelical density in the NAP-deleted strains 23
The ASM fold was influenced differentially in the NAP-deleted strains 24
The AID-induced mutator phenotype of himA and himD mutants is due to R-loop-associated recombination 24
The phenotype of cellular filamentation or elongation in fis, hfq, himA and himD mutants 25
NAP-deleted strains displayed different plasmid-mediated lethality caused by transcription through Sγ3 region 25
Plasmid-mediated lethality caused by transcription through Sγ3 region is reduced after degradation of R-loop 26
The higher copy number of pBR322 in all of the NAP-deleted strains 26
DISCUSSION 28
Reduced R-loop formation in fis mutant may result from decreased global transcription 28
Hfq may prevent nascent RNA from annealing back to template DNA 29
H-NS or StpA itself have no significant impact on R-loop formation 29
The involvement of HU and its homolog IHF in the regulation of R-loop formation 30
TABLES AND FIGURES 32
Table I. Escherichia coli strains used in this study 32
Table II. Plasmids used in this study 33
Table III. Profiles of nucleoid-associated proteins investigated in this study 34
Table IV. Summary of the phenotypes of NAP-deleted strains 35
Figure 1. Plasmid extracted from NAP-deleted strains display different superhelical states in log phase 36
Figure 2. Activation-induced deaminase (AID)-stimulated mutagenesis (ASM) assay. 37
Figure 3. ASM fold of fis, stpA, hupA and hupB mutants are lower than WT and ASM fold of hfq, himA and himD mutants are higher than WT 38

Figure 4. ASM fold of himA and himD mutants, but hfq mutant, are reduced by RNase H overexpression 39
Figure 5. fis mutant revealed heterogeneous cell filamentation and hfq and himA mutant revealed homogeneous cell elongation 40
Figure 6. Quantitative results for the length of bacterail elongation or filamentation 41
Figure 7. After induction of transcription through Sγ3 region, fis, hupA and hupB mutants showed lower plasmid-mediated lethality than WT, but hfq, hns, stpA, himA and himD mutants showed higher plasmid-mediated lethality than WT 42
Figure 8. Compare to mutated RNase H, ectopic overexpression of RNase H reduced plasmid-mediated lethality caused by transcription through Sγ3 region in all of the NAP-deleted strains 43
Figure 9. The copy number of pBR322, a ColE1-origin plasmid, was elevated in all of the NAP-deleted strains 44
Figure 10. A Proposed model for the consequences of excess R-loop formation in the bacteria 45
REFERENCE 46
dc.language.isoen
dc.subject類核體zh_TW
dc.subject基因不穩定性zh_TW
dc.subjectDNA拓樸異構&#37238zh_TW
dc.subject脫氨&#37238zh_TW
dc.subject活化誘導胞嘧啶核&#33527zh_TW
dc.subjectR-loopzh_TW
dc.subject轉錄zh_TW
dc.subject類核體相關蛋白zh_TW
dc.subjectGenome instabilityen
dc.subjectNucleoid-associated proteinsen
dc.subjectTranscriptionen
dc.subjectR-loopen
dc.subjectActivation-induced cytidine deaminase (AID)en
dc.subjectDNA topoisomerasesen
dc.subjectNucleoiden
dc.title探討類核體相關蛋白調控R-loop 之機制與其生物意義zh_TW
dc.titleThe roles of nucleoid-associated proteins in the regulation of R-loop formation and its biological significanceen
dc.typeThesis
dc.date.schoolyear101-2
dc.description.degree碩士
dc.contributor.oralexamcommittee鄧述諄(Shu-Chun Teng),詹世鵬(Shih-Peng Chan)
dc.subject.keyword類核體,類核體相關蛋白,轉錄,R-loop,活化誘導胞嘧啶核&#33527,脫氨&#37238,DNA拓樸異構&#37238,基因不穩定性,zh_TW
dc.subject.keywordNucleoid,Nucleoid-associated proteins,Transcription,R-loop,Activation-induced cytidine deaminase (AID),DNA topoisomerases,Genome instability,en
dc.relation.page60
dc.rights.note有償授權
dc.date.accepted2013-08-16
dc.contributor.author-college醫學院zh_TW
dc.contributor.author-dept微生物學研究所zh_TW
顯示於系所單位:微生物學科所

文件中的檔案:
檔案 大小格式 
ntu-102-1.pdf
  未授權公開取用
18.48 MBAdobe PDF
顯示文件簡單紀錄


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。

社群連結
聯絡資訊
10617臺北市大安區羅斯福路四段1號
No.1 Sec.4, Roosevelt Rd., Taipei, Taiwan, R.O.C. 106
Tel: (02)33662353
Email: ntuetds@ntu.edu.tw
意見箱
相關連結
館藏目錄
國內圖書館整合查詢 MetaCat
臺大學術典藏 NTU Scholars
臺大圖書館數位典藏館
本站聲明
© NTU Library All Rights Reserved