Effects of various single-stranded-DNA-binding proteins on reactions promoted by RecA protein.

Abstract:

:To relate the roles of Escherichia coli SSB in recombination in vivo and in vitro, we have studied the mutant proteins SSB-1 and SSB-113, the variant SSBc produced by chymotryptic cleavage, the partially homologous variant F SSB (encoded by the E. coli sex factor), and the protein encoded by gene 32 of bacteriophage T4. All of these, with the exception of SSB-1, augmented both the initial rate of homologous pairing and strand exchange promoted by RecA protein. From these and related observations, we conclude that SSB stimulates the initial formation of joint molecules by nonspecifically promoting the binding of RecA protein to single-stranded DNA; that SSB plays no role in synapsis of the RecA nucleoprotein filament with duplex DNA; that stimulation of strand exchange by SSB is similarly nonspecific; and that all members of the class of proteins represented by SSB, F SSB, and gene 32 protein may play equivalent roles in making single-stranded DNA more accessible to RecA protein.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Egner C,Azhderian E,Tsang SS,Radding CM,Chase JW

doi

10.1128/jb.169.8.3422-3428.1987

subject

Has Abstract

pub_date

1987-08-01 00:00:00

pages

3422-8

issue

8

eissn

0021-9193

issn

1098-5530

journal_volume

169

pub_type

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