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PMID: 3479792 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Bacteriophage PRD1 DNA polymerase: evolution of DNA polymerases.

Jung GH, Leavitt MC, Hsieh JC, Ito J

Abstract

A small lipid-containing bacteriophage PRD1 specifies its own DNA polymerase that utilizes terminal protein as a primer for DNA synthesis. The PRD1 DNA polymerase gene has been sequenced, and its amino acid sequence has been deduced. This protein-primed DNA polymerase consists of 553 amino acid residues with a calculated molecular weight of 63,300. Thus, it appears to be the smallest DNA polymerase ever isolated from prokaryotic cells. Comparison of the PRD1 DNA polymerase sequence with other DNA polymerase sequences that have been published yielded segmental but significant homologies. These results strongly suggest that many prokaryotic and eukaryotic DNA polymerase genes, regardless of size, have evolved from a common ancestral gene. The results further indicate that those DNA polymerases that use either an RNA or protein primer are related. We propose to classify DNA polymerases on the basis of their evolutionary relatedness.

MeSH Terms
Amino Acid Sequence Bacteriophages/enzymology,genetics Base Sequence Biological Evolution DNA-Directed DNA Polymerase/genetics Molecular Sequence Data Viruses/enzymology,genetics
Chemicals
DNA-Directed DNA Polymerase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Jung G H
Department of Microbiology and Immunology, University of Arizona Health Sciences Center, Tucson 85724.
Leavitt M C
Hsieh J C
Ito J
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1987-12-00
Pages
8287-91
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC299527
Subset
IM
Grants
NIGMS NIH HHS · GM 28013 · United States
Databases
GENBANK
J03018
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