Interaction of the RecA protein of Escherichia coli with single-stranded oligodeoxyribonucleotides.
AUTOR(ES)
Bianco, P R
RESUMO
The RecA protein of Escherichia coli performs a number of ATP-dependent, in vitro reactions and is a DNA-dependent ATPase. Small oligodeoxyribonucleotides were used as DNA cofactors in a kinetic analysis of the ATPase reaction. Polymers of deoxythymidilic acid as well as oligonucleotides of mixed base composition stimulated the RecA ATPase activity in a length-dependent fashion. Both the initial rate and the extent of the reaction were affected by chain length. Full activity was seen with chain lengths > or = 30 nt. Partial activity was seen with chain lengths of 15-30 nt. The lower activity of shorter oligonucleotides was not simply due to a reduced affinity for DNA, since effects of chain length on KmATP and the Hill coefficient for ATP hydrolysis were also observed. The results also suggested that single-stranded DNA secondary structure frequently affects the ATPase activity of RecA protein with oligodeoxyribonucleotides.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=146329Documentos Relacionados
- Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein.
- recA protein-catalyzed strand assimilation: stimulation by Escherichia coli single-stranded DNA-binding protein.
- Purified Escherichia coli recA protein catalyzes homologous pairing of superhelical DNA and single-stranded fragments.
- Hydration of single-stranded phosphodiester and phosphorothioate oligodeoxyribonucleotides.
- Active nucleoprotein filaments of single-stranded binding protein and recA protein on single-stranded DNA have a regular repeating structure.