DNA polymerase V and RecA protein, a minimal mutasome

Katharina Schlacher, Kris Leslie, Claire Wyman, Roger Woodgate, Michael M. Cox, Myron F. Goodman

Research output: Contribution to journalArticlepeer-review

85 Scopus citations

Abstract

A hallmark of the Escherichia coli SOS response is the large increase in mutations caused by translesion synthesis (TLS). TLS requires DNA polymerase V (UmuD′2C) and RecA. Here, we show that pol V and RecA interact by two distinct mechanisms. First, pol V binds to RecA in the absence of DNA and ATP and second, through its UmuD′ subunit, requiring DNA and ATP without ATP hydrolysis. TLS occurs in the absence of a RecA nucleoprotein filament but is inhibited in its presence. Therefore, a RecA nucleoprotein filament is unlikely to be required for SOS mutagenesis. Pol V activity is severely diminished in the absence of RecA or in the presence of RecA1730, a mutant defective for pol V mutagenesis in vivo. Pol V activity is strongly enhanced with RecA mutants constitutive for mutagenesis in vivo, suggesting that RecA is an obligate accessory factor that activates pol V for SOS mutagenesis.

Original languageEnglish (US)
Pages (from-to)561-572
Number of pages12
JournalMolecular cell
Volume17
Issue number4
DOIs
StatePublished - Feb 18 2005
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'DNA polymerase V and RecA protein, a minimal mutasome'. Together they form a unique fingerprint.

Cite this