SSB and the RecG DNA helicase: an intimate association to rescue a stalled replication fork

Piero R. Bianco, Yuri L. Lyubchenko

Research output: Contribution to journalReview articlepeer-review

26 Scopus citations

Abstract

In E. coli, the regression of stalled DNA replication forks is catalyzed by the DNA helicase RecG. One means of gaining access to the fork is by binding to the single strand binding protein or SSB. This interaction occurs via the wedge domain of RecG and the intrinsically disordered linker (IDL) of SSB, in a manner similar to that of SH3 domains binding to PXXP motif-containing ligands in eukaryotic cells. During loading, SSB remodels the wedge domain so that the helicase domains bind to the parental, duplex DNA, permitting the helicase to translocate using thermal energy. This translocation may be used to clear the fork of obstacles, prior to the initiation of fork regression.

Original languageEnglish (US)
Pages (from-to)638-649
Number of pages12
JournalProtein Science
Volume26
Issue number4
DOIs
StatePublished - Apr 1 2017

Keywords

  • DNA repair
  • DNA replication
  • OB-fold
  • PXXP motif
  • RecG
  • SH3 domain
  • SSB
  • atomic force microscopy
  • helicase
  • stalled replication fork

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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