RecA.oligonucleotide filaments bind in the minor groove of double-stranded DNA.
AUTOR(ES)
Baliga, R
RESUMO
Escherichia coli RecA protein, in the presence of ATP or its analog adenosine 5'-[gamma-thio]triphosphate, polymerizes on single-stranded DNA to form nucleoprotein filaments that can then bind to homologous sequences on duplex DNA. The three-stranded joint molecule formed as a result of this binding event is a key intermediate in general recombination. We have used affinity cleavage to examine this three-stranded joint by incorporating a single thymidine-EDTA.Fe (T*) into the oligonucleotide part of the filament. Our analysis of the cleavage patterns from the joint molecule reveals that the nucleoprotein filament binds in the minor groove of an extended Watson-Crick duplex.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=40803Documentos Relacionados
- Intercalators promote the binding of RecA protein to double-stranded DNA.
- Speeding-up the sequencing of double-stranded DNA.
- Kinetics of branch migration in double-stranded DNA.
- Atomic force microscopy of single- and double-stranded DNA.
- The rate of hydrolytic deamination of 5-methylcytosine in double-stranded DNA.