DNA flap creation by the RarA/MgsA protein of Escherichia coli.

Abstract:

:We identify a novel activity of the RarA (also MgsA) protein of Escherichia coli, demonstrating that this protein functions at DNA ends to generate flaps. A AAA+ ATPase in the clamp loader clade, RarA protein is part of a highly conserved family of DNA metabolism proteins. We demonstrate that RarA binds to double-stranded DNA in its ATP-bound state and single-stranded DNA in its apo state. RarA ATPase activity is stimulated by single-stranded DNA gaps and double-stranded DNA ends. At these double-stranded DNA ends, RarA couples the energy of ATP binding and hydrolysis to separating the strands of duplex DNA, creating flaps. We hypothesize that the creation of a flap at the site of a leading strand discontinuity could, in principle, allow DnaB and the associated replisome to continue DNA synthesis without impediment, with leading strand re-priming by DnaG. Replication forks could thus be rescued in a manner that does not involve replisome disassembly or reassembly, albeit with loss of one of the two chromosomal products of a replication cycle.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Stanage TH,Page AN,Cox MM

doi

10.1093/nar/gkw1322

subject

Has Abstract

pub_date

2017-03-17 00:00:00

pages

2724-2735

issue

5

eissn

0305-1048

issn

1362-4962

pii

gkw1322

journal_volume

45

pub_type

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