The Hin recombinase assembles a tetrameric protein swivel that exchanges DNA strands.

ABSTRACT: Most site-specific recombinases can be grouped into two structurally and mechanistically different classes. Whereas recombination by tyrosine recombinases proceeds with little movements by the proteins, serine recombinases exchange DNA strands by a mechanism requiring large quaternary rearrangements. Here we use site-directed crosslinking to investigate the conformational changes that accompany the formation of the synaptic complex and the exchange of DNA strands by the Hin serine recombinase. Efficient crosslinking between residues corresponding to the 'D-helix' region provides the first experimental evidence for interactions between synapsed subunits within this region and distinguishes between different tetrameric conformers that have been observed in crystal structures of related serin

SUBMITTER: Dhar G 

PROVIDER: S-EPMC2724282 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature