RecA acts in trans to allow replication of damaged DNA by DNA polymerase V.

Abstract:

:The DNA polymerase V (pol V) and RecA proteins are essential components of a mutagenic translesion synthesis pathway in Escherichia coli designed to cope with DNA damage. Previously, it has been assumed that RecA binds to the DNA template strand being copied. Here we show, however, that pol-V-catalysed translesion synthesis, in the presence or absence of the beta-processivity-clamp, occurs only when RecA nucleoprotein filaments assemble or RecA protomers bind on separate single-stranded (ss)DNA molecules in trans. A 3'-proximal RecA filament end on trans DNA is essential for stimulation; however, synthesis is strengthened by further pol V-RecA interactions occurring elsewhere along a trans nucleoprotein filament. We suggest that trans-stimulation of pol V by RecA bound to ssDNA reflects a distinctive regulatory mechanism of mutation that resolves the paradox of RecA filaments assembled in cis on a damaged template strand obstructing translesion DNA synthesis despite the absolute requirement of RecA for SOS mutagenesis.

journal_name

Nature

journal_title

Nature

authors

Schlacher K,Cox MM,Woodgate R,Goodman MF

doi

10.1038/nature05042

subject

Has Abstract

pub_date

2006-08-24 00:00:00

pages

883-7

issue

7105

eissn

0028-0836

issn

1476-4687

pii

nature05042

journal_volume

442

pub_type

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