ArticleJournal of molecular biology2008
Modulation of T4 gene 32 protein DNA binding activity by the recombination mediator protein UvsY.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- The bacteriophage T4 homologous recombination system: mechanism, applications, conservation, and environmental significance.EcoSal Plus · 2025Review
- Article
- Mediators of homologous DNA pairing.Cold Spring Harbor perspectives in biology · 2014Review
- Distinct nucleic acid interaction properties of HIV-1 nucleocapsid protein precursor NCp15 explain reduced viral infectivity.Nucleic acids research · 2014Article
- Presynaptic filament dynamics in homologous recombination and DNA repair.Critical reviews in biochemistry and molecular biology · 2011Article
- Assembly and dynamics of the bacteriophage T4 homologous recombination machinery.Virology journal · 2010Review
- Biophysical characterization of DNA binding from single molecule force measurements.Physics of life reviews · 2010Review
- DNA-binding properties of T4 UvsY recombination mediator protein: polynucleotide wrapping promotes high-affinity binding to single-stranded DNA.Nucleic acids research · 2010Article
- Human Rad52 binds and wraps single-stranded DNA and mediates annealing via two hRad52-ssDNA complexes.Nucleic acids research · 2010Article
- The Mei5-Sae3 protein complex mediates Dmc1 activity in Saccharomyces cerevisiae.The Journal of biological chemistry · 2009Article
- Functional complementation of UvsX and UvsY mutations in the mediation of T4 homologous recombination.Nucleic acids research · 2009Article
- Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Bacteriophage T4 UvsY is a recombination mediator protein that promotes assembly of the UvsX-ssDNA presynaptic filament. UvsY helps UvsX to displace T4 gene 32 protein (gp32) from ssDNA, a reaction necessary for proper formation of the presynaptic filament. Here we use DNA stretching to examine UvsY interactions with single DNA molecules in the presence and absence of gp32 and a gp32 C-terminal truncation (*I), and show that in both cases UvsY is able to destabilize gp32-ssDNA interactions. In these experiments UvsY binds more strongly to dsDNA than ssDNA due to its inability to wrap ssDNA at high forces. To support this hypothesis, we show that ssDNA created by exposure of stretched DNA to glyoxal is strongly wrapped by UvsY, but wrapping occurs only at low forces. Our results demonstrate that UvsY interacts strongly with stretched DNA in the absence of other proteins. In the presence of gp32 and *I, UvsY is capable of strongly destabilizing gp32-DNA complexes in order to facilitate ssDNA wrapping, which in turn prepares the ssDNA for presynaptic filament assembly in the presence of UvsX. Thus, UvsY mediates UvsX binding to ssDNA by converting rigid gp32-DNA filaments into a structure that can be strongly bound by UvsX.
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Registered trials
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