Staphylococcus Research Today is a free monthly online journal that collates and summarizes the latest research about Staphylococcus, including details on mrsa, hospitals, infection, antibiotic resistance, superbugs.

Regulation of Sin recombinase by accessory proteins.

Rowland SJ, Boocock MR, Stark WM

University of Glasgow, Institute of Biomedical and Life Sciences, Division of Molecular Genetics, Anderson College, 56 Dumbarton Road, Glasgow G11 6NU, UK. sr2q@udcf.gla.ac.uk

Sin recombinase from Staphylococcus aureus acts selectively on directly repeated resH sites, assembling an intertwined synapse in which exactly three supercoils are trapped between the points of strand exchange. Resolution requires the two Sin binding sites in resH (site I, where strand exchange occurs, and site II) and a non-specific DNA-bending protein (e.g. Hbsu). We show that a single amino acid substitution in Sin (I100T) is sufficient to relax the normal requirements for site II and Hbsu. Using this hyperactive protein, and the variant recombination site resH(AT), we investigate the roles of site II and Hbsu in synapsis and strand exchange. We conclude that Sin bound at site II, and Hbsu, act together to control site I alignment and the topology of the synapse, and to stimulate strand exchange.

Published 7 April 2005 in Mol Microbiol, 56(2): 371-82.
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