Binding of DNA to large fragment of DNA polymerase I: identification of strong and weak electrostatic forces and their biological implications

P N Yadav; J S Yadav; M J Modak

doi:10.1080/07391102.1992.10508649

Binding of DNA to large fragment of DNA polymerase I: identification of strong and weak electrostatic forces and their biological implications

J Biomol Struct Dyn. 1992 Oct;10(2):311-6. doi: 10.1080/07391102.1992.10508649.

Authors

P N Yadav¹, J S Yadav, M J Modak

Affiliation

¹ Department of Biochemistry and Molecular Biology, New Jersey Medical School, University of Medicine and Dentistry of New Jersey, Newark 07103.

PMID: 1466811
DOI: 10.1080/07391102.1992.10508649

Abstract

Examination of the electrostatic potential of a modeled complex, consisting of the Klenow fragment of E. coli DNA polymerase I and DNA template-primer, suggested the presence of two distinct interacting regions. The one displaying a strong electropositive potential field is generated by side chains of basic amino acid pairs and is directed towards the major groove site in DNA. The second electrostatic potential field around DNA is somewhat weaker and appears to be exerted by a pair of vicinal side chains of acidic and basic amino acids. The distribution of charges in this manner appears well suited for the binding of enzyme to the template-primer required in the enzymatic synthesis of DNA.

Publication types

Research Support, U.S. Gov't, P.H.S.

MeSH terms

Binding Sites
DNA / metabolism*
DNA Polymerase I / metabolism*
Electrochemistry
Escherichia coli / enzymology
Templates, Genetic

Substances

DNA
DNA Polymerase I

Grants and funding

NIGMS-36307/GM/NIGMS NIH HHS/United States