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Gene Duplications in Evolution of Archaeal Family B DNA Polymerases

Overview
Journal J Bacteriol
Specialty Microbiology
Date 1997 Apr 1
PMID 9098062
Citations 19
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Abstract

All archaeal DNA-dependent DNA polymerases sequenced to date are homologous to family B DNA polymerases from eukaryotes and eubacteria. Presently, representatives of the euryarchaeote division of archaea appear to have a single family B DNA polymerase, whereas two crenarchaeotes, Pyrodictium occultum and Sulfolobus solfataricus, each possess two family B DNA polymerases. We have found the gene for yet a third family B DNA polymerase, designated B3, in the crenarchaeote S. solfataricus P2. The encoded protein is highly divergent at the amino acid level from the previously characterized family B polymerases in S. solfataricus P2 and contains a number of nonconserved amino acid substitutions in catalytic domains. We have cloned and sequenced the ortholog of this gene from the closely related Sulfolobus shibatae. It is also highly divergent from other archaeal family B DNA polymerases and, surprisingly, from the S. solfataricus B3 ortholog. Phylogenetic analysis using all available archaeal family B DNA polymerases suggests that the S. solfataricus P2 B3 and S. shibatae B3 paralogs are related to one of the two DNA polymerases of P. occultum. These sequences are members of a group which includes all euryarchaeote family B homologs, while the remaining crenarchaeote sequences form another distinct group. Archaeal family B DNA polymerases together constitute a monophyletic subfamily whose evolution has been characterized by a number of gene duplication events.

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References
1.
Wong S, Wahl A, Yuan P, Arai N, Pearson B, Arai K . Human DNA polymerase alpha gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic and eukaryotic replicative DNA polymerases. EMBO J. 1988; 7(1):37-47. PMC: 454213. DOI: 10.1002/j.1460-2075.1988.tb02781.x. View

2.
Nei M, Gojobori T . Simple methods for estimating the numbers of synonymous and nonsynonymous nucleotide substitutions. Mol Biol Evol. 1986; 3(5):418-26. DOI: 10.1093/oxfordjournals.molbev.a040410. View

3.
Hamal A, Forterre P, Elie C . Purification and characterization of a DNA polymerase from the archaebacterium Thermoplasma acidophilum. Eur J Biochem. 1990; 190(3):517-21. DOI: 10.1111/j.1432-1033.1990.tb15604.x. View

4.
Bonner C, Hays S, McEntee K, Goodman M . DNA polymerase II is encoded by the DNA damage-inducible dinA gene of Escherichia coli. Proc Natl Acad Sci U S A. 1990; 87(19):7663-7. PMC: 54808. DOI: 10.1073/pnas.87.19.7663. View

5.
Iwasaki H, Nakata A, Walker G, Shinagawa H . The Escherichia coli polB gene, which encodes DNA polymerase II, is regulated by the SOS system. J Bacteriol. 1990; 172(11):6268-73. PMC: 526809. DOI: 10.1128/jb.172.11.6268-6273.1990. View