Structural basis for transcription-coupled repair: the N terminus of Mfd resembles UvrB with degenerate ATPase motifs

Nora Assenmacher; Katja Wenig; Alfred Lammens; Karl-Peter Hopfner

doi:10.1016/j.jmb.2005.10.033

Structural basis for transcription-coupled repair: the N terminus of Mfd resembles UvrB with degenerate ATPase motifs

J Mol Biol. 2006 Jan 27;355(4):675-83. doi: 10.1016/j.jmb.2005.10.033. Epub 2005 Nov 8.

Authors

Nora Assenmacher¹, Katja Wenig, Alfred Lammens, Karl-Peter Hopfner

Affiliation

¹ Gene Center and Department of Chemistry and Biochemistry, University of Munich (LMU), Feodor-Lynen-Str. 25, D-81377 Munich, Germany.

PMID: 16309703
DOI: 10.1016/j.jmb.2005.10.033

Abstract

The transcription repair coupling factor Mfd removes stalled RNA polymerase from DNA lesions and links transcription to UvrABC-dependent nucleotide excision repair in prokaryotes. We report the 2.1A crystal structure of the UvrA-binding N terminus (residues 1-333) of Escherichia coli Mfd (Mfd-N). Remarkably, Mfd-N reveals a fold that resembles the three N-terminal domains of the repair enzyme UvrB. Domain 1A of Mfd adopts a typical RecA fold, domain 1B matches the damage-binding domain of the UvrB, and domain 2 highly resembles the implicated UvrA-binding domain of UvrB. However, Mfd apparently lacks a functional ATP-binding site and does not contain the DNA damage-binding motifs of UvrB. Thus, our results suggest that Mfd might form a UvrA recruitment factor at stalled transcription complexes that architecturally but not catalytically resembles UvrB.

MeSH terms

Adenosine Triphosphatases / chemistry*
Adenosine Triphosphatases / genetics
Adenosine Triphosphatases / metabolism
Adenosine Triphosphate / chemistry
Amino Acid Sequence
Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Bacterial Proteins / metabolism*
Binding Sites
Conserved Sequence
Crystallography, X-Ray
DNA Helicases / chemistry*
DNA Helicases / genetics
DNA Helicases / metabolism
DNA Repair*
Escherichia coli / enzymology*
Escherichia coli / genetics
Escherichia coli Proteins / chemistry*
Escherichia coli Proteins / genetics
Escherichia coli Proteins / metabolism
Models, Molecular
Molecular Sequence Data
Protein Structure, Tertiary
Rec A Recombinases / chemistry
Rec A Recombinases / metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Structural Homology, Protein
Transcription Factors / chemistry*
Transcription Factors / genetics
Transcription Factors / metabolism*
Transcription, Genetic*

Substances

Bacterial Proteins
Escherichia coli Proteins
Transcription Factors
UvrB protein, E coli
transcription repair coupling factor protein, Bacteria
Adenosine Triphosphate
Rec A Recombinases
Adenosine Triphosphatases
DNA Helicases

Associated data

PDB/2B2N