rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
28
|
pubmed:dateCreated |
1989-10-25
|
pubmed:abstractText |
The bacteriophage T4 uvsY protein is required for efficient recombination in T4-infected Escherichia coli cells. Previous in vitro work has shown that the purified uvsY protein is an accessory protein; it stimulates homologous pairing catalyzed by the phage uvsX protein (a RecA-like recombinase) under certain conditions. We show here that this effect can be traced, at least in part, to a UvsY-dependent stabilization of uvsX protein-single-stranded DNA complexes. These presynaptic filaments are one of the early obligatory intermediates in the strand exchange reaction between homologous single- and double-stranded DNAs. The mechanism of filament stabilization seems to involve a slower loss of UvsX subunits. A model that accounts for the data is presented in which both recombination proteins are incorporated into the presynaptic filament.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0021-9258
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
5
|
pubmed:volume |
264
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
16451-7
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:2550444-Adenosine Triphosphatases,
pubmed-meshheading:2550444-Chromatography,
pubmed-meshheading:2550444-Chromatography, Ion Exchange,
pubmed-meshheading:2550444-DNA-Binding Proteins,
pubmed-meshheading:2550444-Durapatite,
pubmed-meshheading:2550444-Escherichia coli,
pubmed-meshheading:2550444-Hydroxyapatites,
pubmed-meshheading:2550444-Kinetics,
pubmed-meshheading:2550444-Membrane Proteins,
pubmed-meshheading:2550444-Models, Theoretical,
pubmed-meshheading:2550444-Recombination, Genetic,
pubmed-meshheading:2550444-T-Phages,
pubmed-meshheading:2550444-Viral Proteins
|
pubmed:year |
1989
|
pubmed:articleTitle |
The phage T4 uvs Y recombination protein stabilizes presynaptic filaments.
|
pubmed:affiliation |
Department of Chemistry, University of Texas, Austin 78712.
|
pubmed:publicationType |
Journal Article
|