T5 DNA polymerase: structural--functional relationships to other DNA polymerases.
Proc Natl Acad Sci U S A, 1989/6;86(12):4465-9.
Leavitt MC[1], Ito J
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PMID: 2660138
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Abstract
T5 DNA polymerase, a highly processive single-polypeptide enzyme, has been analyzed for its primary structural features. The amino acid sequence of T5 DNA polymerase has a high degree of homology with that of DNA polymerase I from Escherichia coli and retains many of the amino acid residues that have been implicated in the 3'----5' exonuclease and DNA polymerase activities of that enzyme. Alignment with sequences of polymerase I and T7 DNA polymerase was used to identify regions possibly involved in the high processivity of this enzyme. Further, amino acid sequence comparisons of T5 DNA polymerase with a large group of DNA polymerases previously shown to exhibit little similarity to polymerase I indicate certain sequence segments are shared among distantly related DNA polymerases. These shared regions have been implicated in the 3'----5' exonuclease function of polymerase I, which suggests that the proofreading domains of all these enzymes may be evolutionarily related.
MeSH terms
Amino Acid Sequence; Base Sequence; DNA, Viral; DNA-Directed DNA Polymerase; Escherichia coli; Genes; Genes, Viral; Molecular Sequence Data; Restriction Mapping; Sequence Homology, Nucleic Acid; T-Phages
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