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

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′2C). 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 e...

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Bibliographic Details
Published in:BioEssays 2002-02, Vol.24 (2), p.141-148
Main Authors: Gonzalez, Martín, Woodgate, Roger
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
Amino Acid Sequence
ATP-Dependent Proteases
Binding Sites
DNA Polymerase beta - genetics
DNA Polymerase beta - metabolism
DNA-Directed DNA Polymerase
Endopeptidase Clp
Escherichia coli - genetics
Escherichia coli - physiology
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Gene Expression Regulation, Bacterial
Heat-Shock Proteins - genetics
Heat-Shock Proteins - metabolism
Models, Biological
Models, Molecular
Molecular Sequence Data
Mutagenesis
Operon - genetics
Protein Structure, Tertiary
Rec A Recombinases - metabolism
Serine Endopeptidases - genetics
Serine Endopeptidases - metabolism
SOS Response (Genetics)
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Summary: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′2C). 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. BioEssays 24:141–148, 2002. Published 2002 Wiley Periodicals, Inc.
ISSN:0265-9247
1521-1878
DOI:10.1002/bies.10040