Selective disruption of the DNA polymerase III α-β complex by the umuD gene products.

Abstract:

:DNA polymerase III (DNA pol III) efficiently replicates the Escherichia coli genome, but it cannot bypass DNA damage. Instead, translesion synthesis (TLS) DNA polymerases are employed to replicate past damaged DNA; however, the exchange of replicative for TLS polymerases is not understood. The umuD gene products, which are up-regulated during the SOS response, were previously shown to bind to the α, β and ε subunits of DNA pol III. Full-length UmuD inhibits DNA replication and prevents mutagenic TLS, while the cleaved form UmuD' facilitates mutagenesis. We show that α possesses two UmuD binding sites: at the N-terminus (residues 1-280) and the C-terminus (residues 956-975). The C-terminal site favors UmuD over UmuD'. We also find that UmuD, but not UmuD', disrupts the α-β complex. We propose that the interaction between α and UmuD contributes to the transition between replicative and TLS polymerases by removing α from the β clamp.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Silva MC,Nevin P,Ronayne EA,Beuning PJ

doi

10.1093/nar/gks229

subject

Has Abstract

pub_date

2012-07-01 00:00:00

pages

5511-22

issue

12

eissn

0305-1048

issn

1362-4962

pii

gks229

journal_volume

40

pub_type

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