Bacteriophage PRD1 DNA polymerase: evolution of DNA polymerases.

G. H. Jung, M. C. Leavitt, J. C. Hsieh, J. Ito

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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.

Original languageEnglish (US)
Pages (from-to)8287-8291
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume84
Issue number23
DOIs
StatePublished - Dec 1987

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