[Interaction with DNA and aggregation properties of C-terminal fragment of RecA protein].
C-terminal fragment of Escherichia coli RecA protein 150 amino acids residues in length--the product of RecA protein BrCN-hydrolysis--was isolated by single stranded DNA-cellulose chromatography. In low salt buffer this fragment tightly bounds with single and double stranded DNAs. Aggregational properties of the fragment are similar to such of native protein: the fragment oligomerises in low salt buffer and precipitates in the presence of Mg2+. Double stranded DNA in the last case coprecipitates with the fragment, forming a complex which is stable at higher salt concentration, like the complexes with a native RecA protein. These results indicate that the C-terminal half of RecA protein participates in DNA binding and intersubunits interaction of RecA protein.
Volodin
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D001665:Binding Sites; D002850:Chromatography, Gel; D004247:DNA / Q000378:metabolism*; D004277:DNA, Single-Stranded / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D008274:Magnesium; D010446:Peptide Fragments / Q000378:metabolism*; D011938:Rec A Recombinases / Q000378:metabolism*
D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D010446:Peptide Fragments; D004247:DNA; D011938:Rec A Recombinases; D008274:Magnesium
Vzaimodeĭstvie s DNK i agregatsionnye svoĭstva C-kontsevogo fragmenta belka RecA.