The "tale" of UmuD and its role in SOS mutagenesis.

Martín Gonzalez, Roger Woodgate

Journal: BioEssays : news and reviews in molecular, cellular and developmental biology 2002;24(2):141-8

PMID: 11835278

Abstract

Recently, the Escherichia coli umuD and umuC genes have been shown to encode E. coli's fifth DNA polymerase, pol V (consisting of a heterotrimer of UmuD'(2)C). The main function of pol V appears to be the bypass of DNA lesions that would otherwise block replication by pols I-IV. This process is error-prone and leads to a striking increase in mutations at sites of DNA damage. While the enzymatic properties of pol V are now only beginning to be fully appreciated, a great deal is known about how E. coli regulates the intracellular levels of the Umu proteins so that the lesion-bypassing activity of pol V is available to help cells survive the deleterious consequences of DNA damage, yet keeps any unwarranted activity on undamaged templates to a minimum. Our review summarizes the multiple restrictions imposed upon pol V, so as to limit its activity in vivo and, in particular, highlights the pivotal role that the N-terminal tail of UmuD plays in regulating SOS mutagenesis.

Published 2002 Wiley Periodicals, Inc.

Address: Department of Biology, University of Colorado-Denver, Denver, CO, USA.

DOI: 10.1002/bies.10040

Link outs

Free resources

Molecular Biology Databases:

https://ecocyc.org/gene?orgid=ECOLI&id=EG11056

Subscription / membership required

Full Text Sources:

https://doi.org/10.1002/bies.10040

MeSH Terms: ATP-Dependent Proteases, Adenosine Triphosphatases, Amino Acid Sequence, Binding Sites, DNA Polymerase beta, DNA-Directed DNA Polymerase, Endopeptidase Clp, Escherichia coli, Escherichia coli Proteins, Gene Expression Regulation, Bacterial, Heat-Shock Proteins, Models, Biological, Models, Molecular, Molecular Sequence Data, Mutagenesis, Operon, Protein Structure, Tertiary, Rec A Recombinases, SOS Response, Genetics, Serine Endopeptidases