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PMID: 1653031 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

An overview of homologous pairing and DNA strand exchange proteins.

Biochimie ·Vol. 73 ·No. 2-3 ·1991-00-00 ·Pages 163-76

Eggleston AK, Kowalczykowski SC

Abstract

Processes fundamental to all models of genetic recombination include the homologous pairing and subsequent exchange of DNA strands. Biochemical analysis of these events has been conducted primarily on the recA protein of Escherichia coli, although proteins which can promote such reactions have been purified from many sources, both prokaryotic and eukaryotic. The activities of these homologous pairing and DNA strand exchange proteins are either ATP-dependent, as predicted based on the recA protein paradigm, or, more unexpectedly, ATP-independent. This review examines the reactions promoted by both classes of proteins and highlights their similarities and differences. The mechanistic implications of the apparent existence of 2 classes of strand exchange protein are discussed.

MeSH Terms
Adenosine Triphosphatases/metabolism Adenosine Triphosphate/pharmacology Animals Base Composition DNA/metabolism DNA Helicases DNA, Single-Stranded/metabolism Humans Nucleotidyltransferases/metabolism Peptide Hydrolases/metabolism Rec A Recombinases/metabolism Sequence Homology, Nucleic Acid
Chemicals
DNA, Single-Stranded Adenosine Triphosphate DNA Nucleotidyltransferases Rec A Recombinases Peptide Hydrolases Adenosine Triphosphatases DNA Helicases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Eggleston A K
Department of Cell, Molecular, and Structural Biology, Northwestern University Medical School, IL 60611.
Kowalczykowski S C
Article Info
Journal
Biochimie
Abbr.
Biochimie
ISSN
0300-9084
Published
1991-00-00
Pages
163-76
Language
English
Region
France
NLM ID
1264604
Subset
IM
Grants
NIAID NIH HHS · AI-18987 · United States
NIGMS NIH HHS · GM-08061 · United States
NIGMS NIH HHS · GM-41347 · United States
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