On the mechanism of renaturation of complementary DNA strands by the recA protein of Escherichia coli.
AUTOR(ES)
Bryant, F R
RESUMO
The renaturation of complementary DNA strands by the recA protein of Escherichia coli has been found to exhibit the following features. (i) Optimal renaturation occurs at recA protein levels below that required to saturate the DNA strands; saturating amounts of recA protein significantly reduce the rate of reaction. (ii) The reaction proceeds in the absence of a nucleotide cofactor but is markedly stimulated by ATP in the presence of 10 mM Mg2+. A similar stimulation occurs in the absence of ATP when the Mg2+ concentration is increased from 10 mM to 30-40 mM. (iii) Both the ATP-stimulated and the Mg2+-stimulated reactions follow apparent first-order kinetics. These results, taken together with the known effects of ATP and Mg2+ on the state of aggregation of recA protein, suggest that the association of recA monomers may play an important role in recA protein-promoted DNA renaturation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=397024Documentos Relacionados
- ATP-dependent renaturation of DNA catalyzed by the recA protein of Escherichia coli.
- Recombination promoted by superhelical DNA and the recA gene of Escherichia coli.
- Visualization of the paranemic joining of homologous DNA molecules catalyzed by the RecA protein of Escherichia coli.
- Recombinational bypass of pyrimidine dimers promoted by the recA protein of Escherichia coli.
- tif-1 mutation alters polynucleotide recognition by the recA protein of Escherichia coli.
