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PMID: 2823121 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Characterization of an ATP-dependent DNA strand transferase from human cells.

Molecular and cellular biology ·Vol. 7 ·No. 9 ·1987-09-00 ·Pages 3124-30

Ganea D, Moore P, Chekuri L, Kucherlapati R

Abstract

We have characterized an enzymatic activity from human cell nuclei which is capable of catalyzing strand exchange between homologous DNA sequences. The strand exchange activity was Mg2+ dependent and required ATP hydrolysis. In addition, it was capable of promoting reannealing of homologous DNA sequences and could form nucleoprotein networks in a fashion reminiscent of purified bacterial RecA protein. Using an in vitro recombination assay, we also showed that the strand exchange activity was biologically important. The factor(s) responsible for the activity has been partially purified.

MeSH Terms
Adenosine Triphosphatases/isolation & purification,physiology Cell Nucleus/enzymology DNA/metabolism DNA Nucleotidyltransferases Deoxyribonucleoproteins/metabolism Humans Nucleic Acid Renaturation Nucleotidyltransferases/isolation & purification,physiology Recombination, Genetic Sequence Homology, Nucleic Acid
Chemicals
Deoxyribonucleoproteins DNA ATP-dependent DNA strand transferase DNA Nucleotidyltransferases Nucleotidyltransferases Adenosine Triphosphatases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Ganea D
Center for Genetics, University of Illinois College of Medicine, Chicago 60612.
Moore P
Chekuri L
Kucherlapati R
References (34)
34 references, click to expand
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.7.9.3124-3130.1987
Published
1987-09-00
Pages
3124-30
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC367946
Subset
IM
Grants
NCI NIH HHS · CA-37145 · United States
NIGMS NIH HHS · GM-33943 · United States
NIGMS NIH HHS · GM-36565 · United States
External Links
PubMed source DOI: 10.1128/mcb.7.9.3124-3130.1987 PMC Full Text View journal details
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