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PMID: 4610564 Published · ppublish English Journal Article

Properties of the Escherichia coli in DNA binding (unwinding) protein: interaction with DNA polymerase and DNA.

Molineux IJ, Gefter ML

Abstract

The E. coli DNA binding protein reduces the activity of the single-strand-specific nucleases associated with all three DNA polymerases known in E. coli. A slight excess of binding protein over that required to saturate the DNA template leads to total inhibition of activity of the 3' --> 5' nucleases associated with DNA polymerases I and III, but restores maximum activity of the DNA polymerase II-associated nuclease. The binding protein forms a specific complex with DNA polymerase II in the absence of DNA, and it is this complex that degrades a DNA.binding protein complex. Binding protein also facilitates the binding of DNA polymerase II to single-stranded DNA, whereas the binding to DNA of DNA polymerase I is inhibited. These data may explain the specificity with which the binding protein enhances the synthetic ability of DNA polymerase II.

MeSH Terms
Animals Bacterial Proteins/metabolism Cattle Centrifugation, Density Gradient DNA/metabolism DNA Nucleotidyltransferases/metabolism DNA, Single-Stranded/metabolism Escherichia coli/metabolism Protein Binding
Chemicals
Bacterial Proteins DNA, Single-Stranded DNA DNA Nucleotidyltransferases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Molineux I J
Gefter M L
References (9)
9 references, click to expand
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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
1974-10-00
Pages
3858-62
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC434283
Subset
IM
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