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The two functional domains of γδ resolvase act on the same recombination site: Implications for the mechanism of strand exchange

Dröge, P and Hatfull, GF and Grindley, NDF and Cozzarelh, NR (1990) The two functional domains of γδ resolvase act on the same recombination site: Implications for the mechanism of strand exchange. Proceedings of the National Academy of Sciences of the United States of America, 87 (14). 5336 - 5340. ISSN 0027-8424

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Abstract

During site-specific recombination by the γδ resolvase, four DNA strands are broken, exchanged, and religated. This exchange is carried out within a DNA-protein complex, the synaptosome, in which the recombination sites, res, are aligned. The domain of resolvase that binds to a res site is distinct from the domain that breaks and rejoins the DNA. We tested whether the catalytic domain acts on the res site to which its binding domain is bound (in cis) or on the opposing res site in the synaptic complex (in trans). We constructed a hybrid synaptosome in which one res site is bound to wild-type resolvase and the other is bound to a mutant resolvase that binds normally but is unable to break DNA. From the pattern of strand breakage in the reaction intermediate containing resolvase covalently attached to DNA, we conclude that resolvase attacks predominantly, if not exclusively, in cis. Because cis breakage and reunion per se cannot lead to recombination, our results support a model in which DNA exchange is guided by an exchange of resolvase subunits between the breakage and reunion events.


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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Dröge, P
Hatfull, GFgfh@pitt.eduGFH
Grindley, NDF
Cozzarelh, NR
Date: 1 January 1990
Date Type: Publication
Journal or Publication Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 87
Number: 14
Page Range: 5336 - 5340
DOI or Unique Handle: 10.1073/pnas.87.14.5336
Schools and Programs: Dietrich School of Arts and Sciences > Biological Sciences
Refereed: Yes
ISSN: 0027-8424
MeSH Headings: Animals; Crossing Over, Genetic; DNA Replication; Escherichia coli--enzymology; Escherichia coli--genetics; Macromolecular Substances; Models, Genetic; Mutation; Nucleotidyltransferases--genetics; Nucleotidyltransferases--isolation & purification; Nucleotidyltransferases--metabolism; Plasmids; Recombination, Genetic; Restriction Mapping; Synaptosomes--metabolism; Transposases
Other ID: NLM PMC54318
PubMed Central ID: PMC54318
PubMed ID: 2164677
Date Deposited: 01 Mar 2013 15:30
Last Modified: 02 Feb 2019 15:57
URI: http://d-scholarship.pitt.edu/id/eprint/17564

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