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PMID: 3065624 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Holliday intermediates and reaction by-products in FLP protein-promoted site-specific recombination.

Molecular and cellular biology ·Vol. 8 ·No. 9 ·1988-09-00 ·Pages 3784-96

Meyer-Leon L, Huang LC, Umlauf SW, Cox MM, Inman RB

Abstract

Holliday structures are formed and resolved by FLP protein during site-specific recombination. These structures have been isolated and are visualized in both native and partially denatured states by electron microscopy. No single-strand breaks are found within the junction, indicating that the structure results from a reciprocal exchange of strands. These structures have properties consistent with being reaction intermediates. Double-strand cleavage products and "Y structures" are also detected and appear to be by-products of the reaction. The Y structures are three-armed branched molecules with a covalently closed junction located at the FLP recombination target site. Models are discussed, suggesting that both of these novel structures are made by aberrant cleavages during formation and resolution of the Holliday intermediate.

MeSH Terms
Bacterial Outer Membrane Proteins/metabolism DNA/genetics,ultrastructure DNA Nucleotidyltransferases/metabolism Microscopy, Electron Mutation Plasmids Recombination, Genetic Saccharomyces cerevisiae/enzymology,genetics Substrate Specificity
Chemicals
Bacterial Outer Membrane Proteins DNA DNA Nucleotidyltransferases FLP recombinase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Meyer-Leon L
Department of Biochemistry, College of Agriculture and Life Sciences, University of Wisconsin-Madison 53706-1569.
Huang L C
Umlauf S W
Cox M M
Inman R B
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
1988-09-00
Pages
3784-96
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC365437
Subset
IM
Grants
NIGMS NIH HHS · GM14711 · United States
NIGMS NIH HHS · GM37835 · United States
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