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Volumn 17, Issue 1, 2007, Pages 96-102

The bacterial transcription repair coupling factor

Author keywords

[No Author keywords available]

Indexed keywords

ABC EXCINUCLEASE; DOUBLE STRANDED DNA; ENZYME; MOLECULAR MOTOR; RNA POLYMERASE; TRANSCRIPTION REPAIR COUPLING FACTOR; UNCLASSIFIED DRUG;

EID: 33846930416     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2007.01.005     Document Type: Review
Times cited : (30)

References (34)
  • 1
    • 0021905437 scopus 로고
    • DNA repair in an active gene: removal of pyrimidine dimers from the DHFR gene of CHO cells is much more efficient than in the genome overall
    • Bohr V.A., Smith C.A., Okumoto D.S., and Hanawalt P.C. DNA repair in an active gene: removal of pyrimidine dimers from the DHFR gene of CHO cells is much more efficient than in the genome overall. Cell 40 (1985) 359-369
    • (1985) Cell , vol.40 , pp. 359-369
    • Bohr, V.A.1    Smith, C.A.2    Okumoto, D.S.3    Hanawalt, P.C.4
  • 2
    • 0024426244 scopus 로고
    • Induction of the Escherichia coli lactose operon selectively increases repair of its transcribed DNA strand
    • Mellon I., and Hanawalt P.C. Induction of the Escherichia coli lactose operon selectively increases repair of its transcribed DNA strand. Nature 342 (1989) 95-98
    • (1989) Nature , vol.342 , pp. 95-98
    • Mellon, I.1    Hanawalt, P.C.2
  • 3
    • 0023663101 scopus 로고
    • Selective removal of transcription-blocking DNA damage from the transcribed strand of the mammalian DHFR gene
    • Mellon I., Spivak G., and Hanawalt P.C. Selective removal of transcription-blocking DNA damage from the transcribed strand of the mammalian DHFR gene. Cell 51 (1987) 241-249
    • (1987) Cell , vol.51 , pp. 241-249
    • Mellon, I.1    Spivak, G.2    Hanawalt, P.C.3
  • 4
    • 31444444611 scopus 로고    scopus 로고
    • Initiation of DNA repair mediated by a stalled RNA polymerase IIO
    • The authors report the first in vitro reconstitution of eukaryotic TCR.
    • Laine J.P., and Egly J.M. Initiation of DNA repair mediated by a stalled RNA polymerase IIO. EMBO J 25 (2006) 387-397. The authors report the first in vitro reconstitution of eukaryotic TCR.
    • (2006) EMBO J , vol.25 , pp. 387-397
    • Laine, J.P.1    Egly, J.M.2
  • 5
    • 0026354699 scopus 로고
    • Escherichia coli mfd mutant deficient in "mutation frequency decline" lacks strand-specific repair: in vitro complementation with purified coupling factor
    • Selby C.P., Witkin E.M., and Sancar A. Escherichia coli mfd mutant deficient in "mutation frequency decline" lacks strand-specific repair: in vitro complementation with purified coupling factor. Proc Natl Acad Sci USA 88 (1991) 11574-11578
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11574-11578
    • Selby, C.P.1    Witkin, E.M.2    Sancar, A.3
  • 6
    • 0027182114 scopus 로고
    • Helicases: amino acid sequence comparisons and structure-function relationships
    • Gorbalenya A.E., and Koonin E.V. Helicases: amino acid sequence comparisons and structure-function relationships. Curr Opin Struct Biol 3 (1993) 419-429
    • (1993) Curr Opin Struct Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 8
    • 0027905034 scopus 로고
    • Molecular mechanism of transcription-repair coupling
    • Selby C.P., and Sancar A. Molecular mechanism of transcription-repair coupling. Science 260 (1993) 53-58
    • (1993) Science , vol.260 , pp. 53-58
    • Selby, C.P.1    Sancar, A.2
  • 9
    • 0028949551 scopus 로고
    • Structure and function of transcription-repair coupling factor. II. Catalytic properties
    • Selby C.P., and Sancar A. Structure and function of transcription-repair coupling factor. II. Catalytic properties. J Biol Chem 270 (1995) 4890-4895
    • (1995) J Biol Chem , vol.270 , pp. 4890-4895
    • Selby, C.P.1    Sancar, A.2
  • 10
    • 0028969976 scopus 로고
    • Structure and function of transcription-repair coupling factor. I. Structural domains and binding properties
    • Selby C.P., and Sancar A. Structure and function of transcription-repair coupling factor. I. Structural domains and binding properties. J Biol Chem 270 (1995) 4882-4889
    • (1995) J Biol Chem , vol.270 , pp. 4882-4889
    • Selby, C.P.1    Sancar, A.2
  • 11
    • 0035812836 scopus 로고    scopus 로고
    • Structural analysis of DNA replication fork reversal by RecG
    • Singleton M.R., Scaife S., and Wigley D.B. Structural analysis of DNA replication fork reversal by RecG. Cell 107 (2001) 79-89
    • (2001) Cell , vol.107 , pp. 79-89
    • Singleton, M.R.1    Scaife, S.2    Wigley, D.B.3
  • 13
    • 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. E. coli transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation. Cell 109 (2002) 757-767
    • (2002) Cell , vol.109 , pp. 757-767
    • Park, J.-S.1    Marr, M.T.2    Roberts, J.W.3
  • 14
    • 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.J., Ferson A.E., and Fisher S.H. Transcription-repair coupling factor is involved in carbon catabolite repression of the Bacillus subtilis hut and gnt operons. Mol Microbiol 27 (1998) 1031-1038
    • (1998) Mol Microbiol , vol.27 , pp. 1031-1038
    • Zalieckas, J.M.1    Wray, L.V.J.2    Ferson, A.E.3    Fisher, S.H.4
  • 15
    • 0033709634 scopus 로고    scopus 로고
    • Catabolite repression of dra-nupC-pdp operon expression in Bacillus subtilis
    • Zeng X., Galinier A., and Saxild H.H. Catabolite repression of dra-nupC-pdp operon expression in Bacillus subtilis. Microbiology 146 (2000) 2901-2908
    • (2000) Microbiology , vol.146 , pp. 2901-2908
    • Zeng, X.1    Galinier, A.2    Saxild, H.H.3
  • 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. Role of E. coli transcription-repair coupling factor Mfd in Nun-mediated transcription termination. J Mol Biol 329 (2003) 655-662
    • (2003) J Mol Biol , vol.329 , pp. 655-662
    • Washburn, R.S.1    Wang, Y.2    Gottesman, M.E.3
  • 17
    • 22544464455 scopus 로고    scopus 로고
    • RNA polymerase modulators and DNA repair activities resolve conflicts between DNA replication and transcription
    • Trautinger B.W., Jaktaji R.P., Rusakova E., and Lloyd R.G. RNA polymerase modulators and DNA repair activities resolve conflicts between DNA replication and transcription. Mol Cell 19 (2005) 247-258
    • (2005) Mol Cell , vol.19 , pp. 247-258
    • Trautinger, B.W.1    Jaktaji, R.P.2    Rusakova, E.3    Lloyd, R.G.4
  • 18
    • 32044461391 scopus 로고    scopus 로고
    • Crystallization and preliminary structure determination of Escherichia coli Mfd, the transcription-repair coupling factor
    • Deaconescu A.M., and Darst S.A. Crystallization and preliminary structure determination of Escherichia coli Mfd, the transcription-repair coupling factor. Acta Crystallograph Sect F Struct Biol Cryst Commun 61 (2006) 1062-1064
    • (2006) Acta Crystallograph Sect F Struct Biol Cryst Commun , vol.61 , pp. 1062-1064
    • Deaconescu, A.M.1    Darst, S.A.2
  • 19
    • 32044436258 scopus 로고    scopus 로고
    • Structural basis for bacterial transcription-coupled DNA repair
    • This paper describes the 3.2 Å resolution X-ray crystal structure of full-length E. coli TRCF. It also provides a model for a TRCF-TEC complex based on in vivo and in vitro data on a TRCF mutant that is defective in binding RNAP.
    • Deaconescu A.M., Chambers A.L., Smith A.J., Nickels B.E., Hochschild A., Savery N.J., and Darst S.A. Structural basis for bacterial transcription-coupled DNA repair. Cell 124 (2006) 507-520. This paper describes the 3.2 Å resolution X-ray crystal structure of full-length E. coli TRCF. It also provides a model for a TRCF-TEC complex based on in vivo and in vitro data on a TRCF mutant that is defective in binding RNAP.
    • (2006) Cell , vol.124 , pp. 507-520
    • Deaconescu, A.M.1    Chambers, A.L.2    Smith, A.J.3    Nickels, B.E.4    Hochschild, A.5    Savery, N.J.6    Darst, S.A.7
  • 20
    • 29144437721 scopus 로고    scopus 로고
    • Structural basis for transcription-coupled repair: the N-terminus of Mfd resembles UvrB with degenerate ATPase motifs
    • The 2.1 Å resolution X-ray crystal structure of the N terminus (residues 1-333) of E. coli TRCF reveals structural similarity with the N terminus of UvrB.
    • Assenmacher N., Wenig K., Lammens A., and Hopfner K.P. Structural basis for transcription-coupled repair: the N-terminus of Mfd resembles UvrB with degenerate ATPase motifs. J Mol Biol 355 (2006) 675-683. The 2.1 Å resolution X-ray crystal structure of the N terminus (residues 1-333) of E. coli TRCF reveals structural similarity with the N terminus of UvrB.
    • (2006) J Mol Biol , vol.355 , pp. 675-683
    • Assenmacher, N.1    Wenig, K.2    Lammens, A.3    Hopfner, K.P.4
  • 23
    • 0026726828 scopus 로고
    • NusG, a new Escherichia coli elongation factor involved in transcriptional antitermination by the N protein of phage lambda
    • Li J., Horwitz R., McCracken S., and Greenblatt J. NusG, a new Escherichia coli elongation factor involved in transcriptional antitermination by the N protein of phage lambda. J Biol Chem 267 (1992) 6012-6019
    • (1992) J Biol Chem , vol.267 , pp. 6012-6019
    • Li, J.1    Horwitz, R.2    McCracken, S.3    Greenblatt, J.4
  • 24
    • 0034625124 scopus 로고    scopus 로고
    • Regulation of rho-dependent transcription termination by NusG is specific to the Escherichia coli elongation complex
    • Pasman Z., and von Hippel P.H. Regulation of rho-dependent transcription termination by NusG is specific to the Escherichia coli elongation complex. Biochemistry 39 (2000) 5573-5585
    • (2000) Biochemistry , vol.39 , pp. 5573-5585
    • Pasman, Z.1    von Hippel, P.H.2
  • 25
    • 18844457346 scopus 로고    scopus 로고
    • X-ray structures of the Sulfolobus solfataricus SWI2/SNF2 ATPase core and its complex with DNA
    • Durr H., Korner C., Muller M., Hickmann V., and Hopfner K.P. X-ray structures of the Sulfolobus solfataricus SWI2/SNF2 ATPase core and its complex with DNA. Cell 121 (2005) 363-373
    • (2005) Cell , vol.121 , pp. 363-373
    • Durr, H.1    Korner, C.2    Muller, M.3    Hickmann, V.4    Hopfner, K.P.5
  • 26
    • 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. A DNA translocation motif in the bacterial transcription-repair coupling factor, Mfd. Nucleic Acids Res 31 (2003) 6409-6418
    • (2003) Nucleic Acids Res , vol.31 , pp. 6409-6418
    • Chambers, A.L.1    Smith, A.J.2    Savery, N.J.3
  • 27
    • 0037415719 scopus 로고    scopus 로고
    • A model for dsDNA translocation revealed by a structural motif common to RecG and Mfd proteins
    • Mahdi A.A., Briggs G.S., Sharples G.J., Wen Q., and Lloyd R.G. A model for dsDNA translocation revealed by a structural motif common to RecG and Mfd proteins. EMBO J 22 (2003) 724-734
    • (2003) EMBO J , vol.22 , pp. 724-734
    • Mahdi, A.A.1    Briggs, G.S.2    Sharples, G.J.3    Wen, Q.4    Lloyd, R.G.5
  • 28
    • 1842715585 scopus 로고    scopus 로고
    • Forward translocation is the natural pathway of RNA release at an intrinsic terminator
    • Santangelo T.J., and Roberts J.W. Forward translocation is the natural pathway of RNA release at an intrinsic terminator. Mol Cell 14 (2004) 117-126
    • (2004) Mol Cell , vol.14 , pp. 117-126
    • Santangelo, T.J.1    Roberts, J.W.2
  • 29
    • 0037559627 scopus 로고    scopus 로고
    • Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading
    • Skordalakes E., and Berger J.M. Structure of the Rho transcription terminator: mechanism of mRNA recognition and helicase loading. Cell 114 (2003) 135-146
    • (2003) Cell , vol.114 , pp. 135-146
    • Skordalakes, E.1    Berger, J.M.2
  • 30
    • 0344413496 scopus 로고    scopus 로고
    • The flap domain is required for pause RNA hairpin inhibition of catalysis by RNA polymerase and can modulate intrinsic termination
    • Toulokhonov I., and Landick R. The flap domain is required for pause RNA hairpin inhibition of catalysis by RNA polymerase and can modulate intrinsic termination. Mol Cell 12 (2003) 1125-1136
    • (2003) Mol Cell , vol.12 , pp. 1125-1136
    • Toulokhonov, I.1    Landick, R.2
  • 31
    • 33645514260 scopus 로고    scopus 로고
    • Role of DNA bubble rewinding in enzymatic transcription termination
    • Biochemical analyses indicated that DNA bubble rewinding is a prerequisite for Rho- or TRCF-mediated transcription termination. Also, it was shown that forward translocation of RNAP, by either Rho or TRCF, represents an intermediate in RNA release.
    • Park J.S., and Roberts J.W. Role of DNA bubble rewinding in enzymatic transcription termination. Proc Natl Acad Sci USA 103 (2006) 4870-4875. Biochemical analyses indicated that DNA bubble rewinding is a prerequisite for Rho- or TRCF-mediated transcription termination. Also, it was shown that forward translocation of RNAP, by either Rho or TRCF, represents an intermediate in RNA release.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4870-4875
    • Park, J.S.1    Roberts, J.W.2
  • 32
    • 0032478549 scopus 로고    scopus 로고
    • RNA polymerase as a molecular motor
    • Gelles J., and Landick R. RNA polymerase as a molecular motor. Cell 93 (1998) 13-16
    • (1998) Cell , vol.93 , pp. 13-16
    • Gelles, J.1    Landick, R.2
  • 33
  • 34
    • 13844317928 scopus 로고    scopus 로고
    • RNA polymerase mutants defective in the initiation of transcription-coupled DNA repair
    • This paper reports the identification of mutations within the N-terminal domain of the RNAP β-subunit that render RNAP immune to TRCF-mediated release and reactivation of backtracked TECs. The authors proposed that these substitutions affect the initial steps of TCR, namely the recruitment of TRCF to the TEC.
    • Smith A.J., and Savery N.J. RNA polymerase mutants defective in the initiation of transcription-coupled DNA repair. Nucleic Acids Res 33 (2005) 755-764. This paper reports the identification of mutations within the N-terminal domain of the RNAP β-subunit that render RNAP immune to TRCF-mediated release and reactivation of backtracked TECs. The authors proposed that these substitutions affect the initial steps of TCR, namely the recruitment of TRCF to the TEC.
    • (2005) Nucleic Acids Res , vol.33 , pp. 755-764
    • Smith, A.J.1    Savery, N.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.