RecA Protein Promoted Homologous Pairing in Vitro
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چکیده
منابع مشابه
Homologous recognition promoted by RecA protein via
The RecA protein of Escherichia coil forms a nucleoprotein filament that promotes homologous recognition and subsequent strand exchange between a single strand and duplex DNA via a three-stranded intermediate. Recognition of homology within three-stranded nucleoprotein complexes, which is probably central to genetic recombination, is not well understood as compared with the mutual recognition o...
متن کاملRole of superhelicity in homologous pairing of DNA molecules promoted by Escherichia coli recA protein.
In the presence of ATP and an excess of recA protein, superhelical closed circular DNA (form I DNA) and homologous single-stranded fragments paired to form D-loops in the early stage of incubation and dissociated during subsequent incubation. RecA protein that was not bound to single-stranded DNA ("free recA protein") was shown to be responsible for the dissociation of D-loops. Larger amount of...
متن کاملThe search for DNA homology does not limit stable homologous pairing promoted by RecA protein
BACKGROUND The basic molecular mechanisms that govern the search for DNA homology and subsequent homologous pairing during genetic recombination are not understood. RecA is the central homologous recombination protein of Escherichia coli; because several RecA homologues have been identified in eukaryotic cells, it is likely that the mechanisms employed by RecA are conserved throughout evolution...
متن کاملInitiation of genetic recombination: homologous pairing between duplex DNA molecules promoted by recA protein.
recA protein has been shown to promote hydrogen bonding between single-stranded DNA fragments and duplex DNA molecules homologous to them. However, genetic and biochemical evidence indicates that genetic exchanges generally take place between duplex molecules. We therefore chose to study the interactions promoted by recA protein between intact duplex DNA molecules and molecules containing gaps ...
متن کاملrecA protein-promoted ATP hydrolysis occurs throughout recA nucleoprotein filaments.
When recA protein binds cooperatively to single-stranded DNA to form filamentous nucleoprotein complexes, it becomes competent to hydrolyze ATP. No correlation exists between the ends of such complexes and the rate of ATP hydrolysis. ATP hydrolysis is not, therefore, restricted to the terminal subunits on cooperatively bound recA oligomers, but occurs throughout the complex. Similarly, during r...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1989
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)71507-x