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 Resjournal_title
Nucleic acids researchauthors
Silva MC,Nevin P,Ronayne EA,Beuning PJdoi
10.1093/nar/gks229subject
Has Abstractpub_date
2012-07-01 00:00:00pages
5511-22issue
12eissn
0305-1048issn
1362-4962pii
gks229journal_volume
40pub_type
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