Activation of recA protein: the pitch of the helical complex with single-stranded DNA.
AUTOR(ES)
Hewat, E A
RESUMO
The complex of recA protein with single-stranded DNA in the presence of ATP is the active species in the three enzymatic activities of recA: the initiation of strand exchange, the hydrolysis of ATP and the cleavage of repressors. Here we find by cryo-electron microscopy of unstained and unfixed samples that the helical structure of the protein coat in this complex differs slightly but significantly from the structure in the complex with double-stranded DNA. We discuss how the larger pitch of the complex with single strands (100 +/- 2 A compared with 95 +/- 2 A with double strands) could contribute to its higher enzymatic activity.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=452972Documentos Relacionados
- Isolation and visualization of active presynaptic filaments of recA protein and single-stranded DNA.
- Active nucleoprotein filaments of single-stranded binding protein and recA protein on single-stranded DNA have a regular repeating structure.
- Recognition of duplex DNA containing single-stranded regions by recA protein.
- Interaction of the RecA protein of Escherichia coli with single-stranded oligodeoxyribonucleotides.
- The RecOR proteins modulate RecA protein function at 5′ ends of single-stranded DNA