E. coli Transcription Repair Coupling Factor (Mfd Protein) Rescues Arrested Complexes by Promoting Forward Translocation

Transcription and DNA repair are coupled in E. coli by the Mfd protein, which dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. We show that Mfd influences the elongation state of RNA polymerase (RNAP); transcription complexes that have reverse translocated into the backtracked position, a potentially important intermediate in RNA proofreading and repair, are restored to the forward position by the activity of Mfd, and arrested complexes are rescued into productive elongation. Mfd may act through a translocase activity that rewinds upstream DNA, leading either to translocation or to release of RNA polymerase when the enzyme active site cannot continue elongation.

[1]  E. Witkin Mutation frequency decline revisited. , 1994, BioEssays : news and reviews in molecular, cellular and developmental biology.

[2]  A. Sancar,et al.  Mechanisms of transcription-repair coupling and mutation frequency decline. , 1994, Microbiological reviews.

[3]  D. Wigley,et al.  Structural Analysis of DNA Replication Fork Reversal by RecG , 2001, Cell.

[4]  D. Lilley,et al.  Mechanisms of Transcription , 1997, Nucleic Acids and Molecular Biology.

[5]  N. Fujita,et al.  Organization of open complexes at Escherichia coli promoters. Location of promoter DNA sites close to region 2.5 of the sigma70 subunit of RNA polymerase. , 1999, The Journal of biological chemistry.

[6]  S. Fisher,et al.  Transcription–repair coupling factor is involved in carbon catabolite repression of the Bacillus subtilis hut and gnt operons , 1998, Molecular microbiology.

[7]  J. Svejstrup Transcription: Mechanisms of transcription-coupled DNA repair , 2002, Nature Reviews Molecular Cell Biology.

[8]  A. Sancar,et al.  Structure and Function of Transcription-Repair Coupling Factor , 1995, The Journal of Biological Chemistry.

[9]  M. Susskind,et al.  A mutant Escherichia coli sigma 70 subunit of RNA polymerase with altered promoter specificity. , 1989, Journal of molecular biology.

[10]  P. Cramer,et al.  Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution , 2001, Science.

[11]  M. Kashlev,et al.  Functional topography of nascent RNA in elongation intermediates of RNA polymerase. , 1998, Proceedings of the National Academy of Sciences of the United States of America.

[12]  R. G. Lloyd,et al.  Branch migration of Holliday junctions: identification of RecG protein as a junction specific DNA helicase. , 1994, The EMBO journal.

[13]  S. Borukhov,et al.  Purification and assay of Escherichia coli transcript cleavage factors GreA and GreB. , 1996, Methods in enzymology.

[14]  Jeffrey W. Roberts,et al.  Restructuring of an RNA polymerase holoenzyme elongation complex by lambdoid phage Q proteins , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[15]  Jeffrey W. Roberts,et al.  Mechanism of intrinsic transcription termination and antitermination. , 1999, Science.

[16]  W. Mangel,et al.  RNA polymerase , 2020, Nature.

[17]  M. Kashlev,et al.  Transcriptional arrest: Escherichia coli RNA polymerase translocates backward, leaving the 3' end of the RNA intact and extruded. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[18]  A. Sancar,et al.  Structure and Function of Transcription-Repair Coupling Factor , 1995, The Journal of Biological Chemistry.

[19]  P. Cramer,et al.  Structural Basis of Transcription: An RNA Polymerase II Elongation Complex at 3.3 Å Resolution , 2001, Science.

[20]  K. Severinov,et al.  The Largest Subunits of RNA Polymerase from Gastric Helicobacters Are Tethered* , 1998, The Journal of Biological Chemistry.

[21]  R. Young,et al.  RNA polymerase II. , 1991, Annual review of biochemistry.

[22]  E. Nudler,et al.  Coupling between transcription termination and RNA polymerase inchworming , 1995, Cell.

[23]  P. Modrich,et al.  The negative charge of Glu-111 is required to activate the cleavage center of EcoRI endonuclease. , 1989, The Journal of biological chemistry.

[24]  P. V. von Hippel,et al.  Multiple RNA polymerase conformations and GreA: control of the fidelity of transcription. , 1993, Science.

[25]  E. Nudler,et al.  The RNA–DNA Hybrid Maintains the Register of Transcription by Preventing Backtracking of RNA Polymerase , 1997, Cell.

[26]  J. Hoeijmakers,et al.  Cockayne syndrome: defective repair of transcription? , 1997, The EMBO journal.

[27]  M. Kashlev,et al.  RNA Polymerase Switches between Inactivated and Activated States By Translocating Back and Forth along the DNA and the RNA* , 1997, The Journal of Biological Chemistry.

[28]  James C. Hu,et al.  Altered promoter recognition by mutant forms of the sigma 70 subunit of Escherichia coli RNA polymerase. , 1989, Journal of molecular biology.

[29]  J. Wojcik,et al.  The protein–protein interaction map of Helicobacter pylori , 2001, Nature.

[30]  M. Chamberlin,et al.  Transcription elongation factor SII (TFIIS) enables RNA polymerase II to elongate through a block to transcription in a human gene in vitro. , 1989, The Journal of biological chemistry.

[31]  Jeffrey W. Roberts,et al.  The phage λ gene Q transcription antiterminator binds DNA in the late gene promoter as it modifies RNA polymerase , 1992, Cell.

[32]  A. Sancar,et al.  Cockayne syndrome group B protein enhances elongation by RNA polymerase II. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[33]  Jeffrey W. Roberts,et al.  Function of E. coli RNA Polymerase σ Factor- σ70 in Promoter-Proximal Pausing , 1996, Cell.

[34]  S. Borukhov,et al.  Transcript cleavage factors from E. coli , 1993, Cell.

[35]  C. Hovens,et al.  An In Vitro Assay of β-Galactosidase from Yeast , 1996 .

[36]  J M Rosenberg,et al.  Refinement of Eco RI endonuclease crystal structure: a revised protein chain tracing. , 1990, Science.

[37]  A. Sancar,et al.  Molecular mechanism of transcription-repair coupling. , 1993, Science.

[38]  S. Darst,et al.  A Structural Model of Transcription Elongation , 2000 .

[39]  S. Borukhov,et al.  GreA protein: a transcription elongation factor from Escherichia coli. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[40]  Satya Prakash,et al.  Requirement for Yeast RAD26, a Homolog of the HumanCSB Gene, in Elongation by RNA Polymerase II , 2001, Molecular and Cellular Biology.

[41]  D. Price,et al.  Drosophila Factor 2, an RNA Polymerase II Transcript Release Factor, Has DNA-dependent ATPase Activity* , 1997, The Journal of Biological Chemistry.

[42]  J. Roberts,et al.  Function of transcription cleavage factors GreA and GreB at a regulatory pause site. , 2000, Molecular cell.

[43]  K. Severinov,et al.  Crystal Structure of Thermus aquaticus Core RNA Polymerase at 3.3 Å Resolution , 1999, Cell.