Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein.
نویسندگان
چکیده
منابع مشابه
The process of displacing the single-stranded DNA-binding protein from single-stranded DNA by RecO and RecR proteins
The regions of single-stranded (ss) DNA that result from DNA damage are immediately coated by the ssDNA-binding protein (SSB). RecF pathway proteins facilitate the displacement of SSB from ssDNA, allowing the RecA protein to form protein filaments on the ssDNA region, which facilitates the process of recombinational DNA repair. In this study, we examined the mechanism of SSB displacement from s...
متن کاملContinuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA.
The single-stranded DNA binding protein of Escherichia coli (SSB) stimulates recA protein promoted DNA strand exchange reactions by promoting and stabilizing the interaction between recA protein and single-stranded DNA (ssDNA). Utilizing the intrinsic tryptophan fluorescence of SSB, an ATP-dependent interaction has been detected between SSB and recA-ssDNA complexes. This interaction is continuo...
متن کاملStabilization of recA protein-ssDNA complexes by the single-stranded DNA binding protein of Escherichia coli.
In vitro recombination reactions promoted by the recA protein of Escherichia coli are enhanced by the single-stranded DNA binding protein (SSB). SSB affects the assembly of the filamentous complexes between recA protein and ssDNA that are the active form of the recA protein. Here, we present evidence that SSB plays a complex role in maintaining the stability and activity of recA-ssDNA filaments...
متن کاملThe C terminus of the Escherichia coli RecA protein modulates the DNA binding competition with single-stranded DNA-binding protein.
The nucleation step of Escherichia coli RecA filament formation on single-stranded DNA (ssDNA) is strongly inhibited by prebound E. coli ssDNA-binding protein (SSB). The capacity of RecA protein to displace SSB is dramatically enhanced in RecA proteins with C-terminal deletions. The displacement of SSB by RecA protein is progressively improved when 6, 13, and 17 C-terminal amino acids are remov...
متن کاملInteraction of the recA protein of Escherichia coli with single-stranded DNA.
The interaction of recA protein with single-stranded (ss) phi X174 DNA has been examined by means of a nuclease protection assay. The stoichiometry of protection was found to be 1 recA monomer/approximately 4 nucleotides of ssDNA both in the absence of a nucleotide cofactor and in the presence of ATP. In contrast, in the presence of adenosine 5'-O-(thiotriphosphate) (ATP gamma S) the stoichiome...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1993
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.90.9.3875