Human and mouse homologs of Escherichia coli DinB (DNA polymerase IV), members of the UmuC/DinB superfamily

Valerie L. Gerlach, L. Aravind, Garrett Gotway, Roger A. Schultz, Eugene V. Koonin, Errol C. Friedberg

Research output: Contribution to journalArticle

183 Citations (Scopus)

Abstract

To understand the mechanisms underlying mutagenesis in eukaryotes better, we have cloned mouse and human homologs of the Escherichia coli dinB gene. E. coli dinB encodes DNA polymerase IV and greatly increases spontaneous mutations when overexpressed. The mouse and human DinB1 amino acid sequences share significant identity with E. coli DinB, including distinct motifs implicated in catalysis, suggesting conservation of the polymerase function. These proteins are members of a large superfamily of DNA damage-bypass replication proteins, including the E. coli proteins UmuC and DinB and the Saccharomyces cerevisiae proteins Rev1 and Rad30. In a phylogenetic tree, the mouse and human DinB1 proteins specifically group with E. coli DinB, suggesting a mitochondrial origin for these genes. The human DINB1 gene is localized to chromosome 5q13 and is widely expressed.

Original languageEnglish (US)
Pages (from-to)11922-11927
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume96
Issue number21
DOIs
StatePublished - Oct 12 1999

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DNA Polymerase beta
Escherichia coli
Saccharomyces cerevisiae Proteins
Mitochondrial Genes
Eukaryota
Catalysis
Mutagenesis
Genes
DNA Damage
Amino Acid Sequence
Proteins
Chromosomes
Mutation

ASJC Scopus subject areas

  • Genetics
  • General

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Human and mouse homologs of Escherichia coli DinB (DNA polymerase IV), members of the UmuC/DinB superfamily. / Gerlach, Valerie L.; Aravind, L.; Gotway, Garrett; Schultz, Roger A.; Koonin, Eugene V.; Friedberg, Errol C.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, No. 21, 12.10.1999, p. 11922-11927.

Research output: Contribution to journalArticle

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