메뉴 건너뛰기




Volumn 33, Issue 2, 2005, Pages 755-764

RNA polymerase mutants defective in the initiation of transcription-coupled DNA repair

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; RNA POLYMERASE; DNA DIRECTED RNA POLYMERASE; ESCHERICHIA COLI PROTEIN; RNA POLYMERASE BETA SUBUNIT; TRANSCRIPTION FACTOR; TRANSCRIPTION REPAIR COUPLING FACTOR PROTEIN, BACTERA;

EID: 13844317928     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gki225     Document Type: Article
Times cited : (50)

References (44)
  • 1
    • 0034026376 scopus 로고    scopus 로고
    • RNA polymerase structure-function: Insights into points of transcriptional regulation
    • Severinov,K. (2000) RNA polymerase structure-function: insights into points of transcriptional regulation. Curr. Opin. Microbiol., 3, 118-125.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 118-125
    • Severinov, K.1
  • 2
    • 0038013991 scopus 로고    scopus 로고
    • RNA polymerase holoenzyme: Structure, function and biological implications
    • Borukhov,S. and Nudler,E. (2003) RNA polymerase holoenzyme: structure, function and biological implications. Curr. Opin. Microbiol., 6, 93-100.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 93-100
    • Borukhov, S.1    Nudler, E.2
  • 3
    • 0034671288 scopus 로고    scopus 로고
    • RNA polymerase: Structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II
    • Ebright,R.H. (2000) RNA polymerase: structural similarities between bacterial RNA polymerase and eukaryotic RNA polymerase II. J. Mol. Biol., 304, 687-698.
    • (2000) J. Mol. Biol. , vol.304 , pp. 687-698
    • Ebright, R.H.1
  • 5
    • 2542428546 scopus 로고    scopus 로고
    • Structure and mechanism of the RNA polymerase II transcription machinery
    • Hahn,S. (2004) Structure and mechanism of the RNA polymerase II transcription machinery. Nature Struct. Mol. Biol., 11, 394-403.
    • (2004) Nature Struct. Mol. Biol. , vol.11 , pp. 394-403
    • Hahn, S.1
  • 6
    • 0028969976 scopus 로고
    • Structure and function of transcription-repair coupling factor. I. Structural domains and binding properties
    • Selby,C.P. and Sancar,A. (1995) Structure and function of transcription-repair coupling factor. I. Structural domains and binding properties. J. Biol. Chem., 270, 4882-4889.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4882-4889
    • Selby, C.P.1    Sancar, A.2
  • 7
    • 0028949551 scopus 로고
    • Structure and function of transcription-repair coupling factor. II. Catalytic properties
    • Selby,C.P. and Sancar,A. (1995) Structure and function of transcription-repair coupling factor. II. Catalytic properties. J. Biol. Chem., 270, 4890-4895.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4890-4895
    • Selby, C.P.1    Sancar, A.2
  • 8
    • 0027905034 scopus 로고
    • Molecular mechanism of transcription-repair coupling
    • Selby,C.P. and Sancar,A. (1993) Molecular mechanism of transcription-repair coupling. Science, 260, 53-58.
    • (1993) Science , vol.260 , pp. 53-58
    • Selby, C.P.1    Sancar, A.2
  • 9
    • 0037077154 scopus 로고    scopus 로고
    • E.coli transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation
    • Park,J.S., Marr,M.T. and Roberts,J.W. (2002) E.coli transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation. Cell, 109, 757-767.
    • (2002) Cell , vol.109 , pp. 757-767
    • Park, J.S.1    Marr, M.T.2    Roberts, J.W.3
  • 10
    • 0345531143 scopus 로고    scopus 로고
    • A DNA translocation motif in the bacterial transcription-repair coupling factor, Mfd
    • Chambers,A.L., Smith,A.J. and Savery,N.J. (2003) A DNA translocation motif in the bacterial transcription-repair coupling factor, Mfd. Nucleic Acids Res., 31, 6409-6418.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6409-6418
    • Chambers, A.L.1    Smith, A.J.2    Savery, N.J.3
  • 11
    • 0033709634 scopus 로고    scopus 로고
    • Catabolite repression of dra-nupC-pdp operon expression in Bacillus subtilis
    • Zeng,X., Galinier,A. and Saxild,H.H. (2000) Catabolite repression of dra-nupC-pdp operon expression in Bacillus subtilis. Microbiology, 146, 2901-2908.
    • (2000) Microbiology , vol.146 , pp. 2901-2908
    • Zeng, X.1    Galinier, A.2    Saxild, H.H.3
  • 12
    • 0031779321 scopus 로고    scopus 로고
    • Transcription-repair coupling factor is involved in carbon catabolite repression of the Bacillus subtilis hut and gnt operons
    • Zalieckas,J.M., Wray,L.V.,Jr, Ferson,A.E. and Fisher,S.H. (1998) Transcription-repair coupling factor is involved in carbon catabolite repression of the Bacillus subtilis hut and gnt operons. Mol. Microbiol., 27, 1031-1038.
    • (1998) Mol. Microbiol. , vol.27 , pp. 1031-1038
    • Zalieckas, J.M.1    Wray Jr., L.V.2    Ferson, A.E.3    Fisher, S.H.4
  • 13
    • 0345938313 scopus 로고
    • Lac Repressor blocks transcribing RNA polymerase and terminates transcription
    • Deuschle,U., Gentz,R. and Bujard,H. (1986) lac Repressor blocks transcribing RNA polymerase and terminates transcription. Proc. Natl Acad. Sci. USA, 83, 4134-4137.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4134-4137
    • Deuschle, U.1    Gentz, R.2    Bujard, H.3
  • 14
    • 0027421132 scopus 로고
    • Transcription-repair coupling and mutation frequency decline
    • Selby,C.P. and Sancar,A. (1993) Transcription-repair coupling and mutation frequency decline. J. Bacteriol., 175, 7509-7514.
    • (1993) J. Bacteriol. , vol.175 , pp. 7509-7514
    • Selby, C.P.1    Sancar, A.2
  • 15
    • 0028988448 scopus 로고
    • Phage HK022 Nun protein arrests transcription on phage lambda DNA in vitro and competes with the phage lambda N antitermination protein
    • Hung,S.C. and Gottesman,M.E. (1995) Phage HK022 Nun protein arrests transcription on phage lambda DNA in vitro and competes with the phage lambda N antitermination protein. J. Mol. Biol., 247, 428-442.
    • (1995) J. Mol. Biol. , vol.247 , pp. 428-442
    • Hung, S.C.1    Gottesman, M.E.2
  • 16
    • 0037716599 scopus 로고    scopus 로고
    • Role of E.coli Transcription-repair coupling factor Mfd in Nun-mediated transcription termination
    • Washburn,R.S., Wang,Y. and Gottesman,M.E. (2003) Role of E.coli Transcription-repair coupling factor Mfd in Nun-mediated transcription termination. J. Mol. Biol., 329, 655-662.
    • (2003) J. Mol. Biol. , vol.329 , pp. 655-662
    • Washburn, R.S.1    Wang, Y.2    Gottesman, M.E.3
  • 17
    • 0031059249 scopus 로고    scopus 로고
    • Transcriptional arrest: Escherichia coli RNA polymerase translocates backward, leaving the 3′ end of the RNA intact and extruded
    • Komissarova,N. and Kashlev,M. (1997) Transcriptional arrest: Escherichia coli RNA polymerase translocates backward, leaving the 3′ end of the RNA intact and extruded. Proc. Natl Acad. Sci. USA, 94, 1755-1760.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1755-1760
    • Komissarova, N.1    Kashlev, M.2
  • 18
    • 0027536870 scopus 로고
    • Transcript cleavage factors from E.coli
    • Borukhov,S., Sagitov,V. and Goldfarb,A. (1993) Transcript cleavage factors from E.coli. Cell, 72, 459-466.
    • (1993) Cell , vol.72 , pp. 459-466
    • Borukhov, S.1    Sagitov, V.2    Goldfarb, A.3
  • 19
    • 0035812836 scopus 로고    scopus 로고
    • Structural analysis of DNA replication fork reversal by RecG
    • Singleton,M.R., Scaife,S. and Wigley,D.B. (2001) Structural analysis of DNA replication fork reversal by RecG. Cell, 107, 79-89.
    • (2001) Cell , vol.107 , pp. 79-89
    • Singleton, M.R.1    Scaife, S.2    Wigley, D.B.3
  • 20
    • 1842610540 scopus 로고    scopus 로고
    • Mfd, the bacterial transcription repair coupling factor: Translocation, repair and termination
    • Roberts,J. and Park,J.S. (2004) Mfd, the bacterial transcription repair coupling factor: translocation, repair and termination. Curr. Opin. Microbiol., 7, 120-125.
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 120-125
    • Roberts, J.1    Park, J.S.2
  • 22
    • 0037123659 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution
    • Murakami,K.S., Masuda,S. and Darst,S.A. (2002) Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 Å resolution. Science, 296, 1280-1284.
    • (2002) Science , vol.296 , pp. 1280-1284
    • Murakami, K.S.1    Masuda, S.2    Darst, S.A.3
  • 23
    • 0027320544 scopus 로고
    • Rifampicin region revisited. New rifampicin-resistant and streptolydigin-resistant mutants in the beta subunit of Escherichia coli RNA polymerase
    • Severinov,K., Soushko,M., Goldfarb,A. and Nikiforov,V. (1993) Rifampicin region revisited. New rifampicin-resistant and streptolydigin-resistant mutants in the beta subunit of Escherichia coli RNA polymerase. J. Biol. Chem., 268, 14820-14825.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14820-14825
    • Severinov, K.1    Soushko, M.2    Goldfarb, A.3    Nikiforov, V.4
  • 25
    • 0034698044 scopus 로고    scopus 로고
    • Interaction between RNA polymerase and RapA, a bacterial homolog of the SWI/SNF protein family
    • Sukhodolets,M.V. and Jin,D.J. (2000) Interaction between RNA polymerase and RapA, a bacterial homolog of the SWI/SNF protein family. J. Biol. Chem., 275, 22090-22097.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22090-22097
    • Sukhodolets, M.V.1    Jin, D.J.2
  • 26
    • 0030582675 scopus 로고    scopus 로고
    • Transcription activation at class H CAP-dependent promoters: Two interactions between CAP and RNA polymerase
    • Niu,W., Kim,Y., Tau,G., Heyduk,T. and Ebright,R.H. (1996) Transcription activation at class H CAP-dependent promoters: two interactions between CAP and RNA polymerase. Cell, 87, 1123-1134.
    • (1996) Cell , vol.87 , pp. 1123-1134
    • Niu, W.1    Kim, Y.2    Tau, G.3    Heyduk, T.4    Ebright, R.H.5
  • 27
    • 0032526956 scopus 로고    scopus 로고
    • Transcription activation at Class II CRP-dependent promoters: Identification of determinants in the C-terminal domain of the RNA polymerase alpha subunit
    • Savery,N.J., Lloyd,G.S., Kainz,M., Gaal,T., Ross,W., Ebright,R.H., Gourse,R.L. and Busby,S.J. (1998) Transcription activation at Class II CRP-dependent promoters: identification of determinants in the C-terminal domain of the RNA polymerase alpha subunit. EMBO J., 17, 3439-3447.
    • (1998) EMBO J. , vol.17 , pp. 3439-3447
    • Savery, N.J.1    Lloyd, G.S.2    Kainz, M.3    Gaal, T.4    Ross, W.5    Ebright, R.H.6    Gourse, R.L.7    Busby, S.J.8
  • 28
    • 0023645129 scopus 로고
    • Isolation and properties of transcribing ternary complexes of Escherichia coli RNA polymerase positioned at a single template base
    • Levin,J.R., Krummel,B. and Chamberlin,M.J. (1987) Isolation and properties of transcribing ternary complexes of Escherichia coli RNA polymerase positioned at a single template base. J. Mol. Biol. 196, 85-100.
    • (1987) J. Mol. Biol. , vol.196 , pp. 85-100
    • Levin, J.R.1    Krummel, B.2    Chamberlin, M.J.3
  • 30
    • 0027496935 scopus 로고
    • The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases
    • Harper,J.W., Adami,G.R., Wei,N., Keyomarsi,K. and Elledge,S.J. (1993) The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell, 75, 805-816.
    • (1993) Cell , vol.75 , pp. 805-816
    • Harper, J.W.1    Adami, G.R.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.J.5
  • 31
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz,D., St Jean,A., Woods,R.A. and Schiestl,R.H. (1992) Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res., 20, 1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 32
    • 0036270928 scopus 로고    scopus 로고
    • LacZ assays in yeast
    • Rupp,S. (2002) LacZ assays in yeast. Methods Enzymol., 350, 112-131.
    • (2002) Methods Enzymol. , vol.350 , pp. 112-131
    • Rupp, S.1
  • 33
    • 0033578701 scopus 로고    scopus 로고
    • Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution
    • Zhang,G., Campbell,E.A., Minakhin,L., Richter,C., Severinov,K. and Darst,S.A. (1999) Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 Å resolution. Cell, 98, 811-824.
    • (1999) Cell , vol.98 , pp. 811-824
    • Zhang, G.1    Campbell, E.A.2    Minakhin, L.3    Richter, C.4    Severinov, K.5    Darst, S.A.6
  • 34
    • 0035970037 scopus 로고    scopus 로고
    • Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly
    • Minakhin,L., Bhagat,S., Brunning,A., Campbell,E.A., Darst,S.A., Ebright,R.H. and Severinov,K. (2001) Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly. Proc. Natl Acad. Sci. USA, 98, 892-897.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 892-897
    • Minakhin, L.1    Bhagat, S.2    Brunning, A.3    Campbell, E.A.4    Darst, S.A.5    Ebright, R.H.6    Severinov, K.7
  • 35
    • 0029939231 scopus 로고    scopus 로고
    • The Mfd protein of Bacillus subtilis 168 is involved in both transcription-coupled DNA repair and DNA recombination
    • Ayora,S., Rojo,F., Ogasawara,N., Nakai,S. and Alonso,J.C. (1996) The Mfd protein of Bacillus subtilis 168 is involved in both transcription-coupled DNA repair and DNA recombination. J. Mol. Biol. 256, 301-318.
    • (1996) J. Mol. Biol. , vol.256 , pp. 301-318
    • Ayora, S.1    Rojo, F.2    Ogasawara, N.3    Nakai, S.4    Alonso, J.C.5
  • 36
    • 0345884910 scopus 로고    scopus 로고
    • Methods of walking with the RNA polymerase
    • Nudler,E., Gusarov,I. and Bar-Nahum,G. (2003) Methods of walking with the RNA polymerase. Methods Enzymol., 371, 160-169.
    • (2003) Methods Enzymol. , vol.371 , pp. 160-169
    • Nudler, E.1    Gusarov, I.2    Bar-Nahum, G.3
  • 37
    • 0029818631 scopus 로고    scopus 로고
    • Transcription processivity: Protein-DNA interactions holding together the elongation complex
    • Nudler,E., Avetissova,E., Markovtsov,V. and Goldfarb,A. (1996) Transcription processivity: protein-DNA interactions holding together the elongation complex. Science, 273, 211-217.
    • (1996) Science , vol.273 , pp. 211-217
    • Nudler, E.1    Avetissova, E.2    Markovtsov, V.3    Goldfarb, A.4
  • 38
    • 0028095381 scopus 로고
    • Mechanisms of transcription-repair coupling and mutation frequency decline
    • Selby,C.P. and Sancar,A. (1994) Mechanisms of transcription-repair coupling and mutation frequency decline. Microbiol. Rev., 58, 317-329.
    • (1994) Microbiol. Rev. , vol.58 , pp. 317-329
    • Selby, C.P.1    Sancar, A.2
  • 39
    • 0014004977 scopus 로고
    • Radiation-induced mutations and their repair
    • Witkin,E.M. (1966) Radiation-induced mutations and their repair. Science, 152, 1345-1353.
    • (1966) Science , vol.152 , pp. 1345-1353
    • Witkin, E.M.1
  • 40
    • 0037123602 scopus 로고    scopus 로고
    • Structural basis of transcription initiation: An RNA polymerase holoenzyme-DNA complex
    • Murakami,K.S., Masuda,S., Campbell,E.A., Muzzin,O. and Darst,S.A. (2002) Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex. Science, 296, 1285-1290.
    • (2002) Science , vol.296 , pp. 1285-1290
    • Murakami, K.S.1    Masuda, S.2    Campbell, E.A.3    Muzzin, O.4    Darst, S.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.