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Papers In Press, published online ahead of print April 28, 2003
Department of Biochemistry, University of Utah-School of Medicine, Salt Lake City, UT 84132-3201
Corresponding Author: Janet.Lindsley{at}hsc.utah.edu
To better understand the contributions that the Structural Maintenance of Chromosome proteins (SMCs) make to condensin activity, we have tested a number of biochemical, biophysical and DNA-associated attributes of the Smc2p-Smc4p pair from budding yeast. Smc2p and Smc4p form a stable heterodimer, the "Smc2/4 complex", which upon analysis by sedimentation equilibrium appears to reversibly self-associate to form heterotetramers. Individually, neither Smc2p nor Smc4p hydrolyze ATP; however, ATPase activity is recovered by equal molar mixing of both purified proteins. Hydrolysis activity is unaffected by the presence of DNA. Smc2/4 binds both linearized and circular plasmids, and the binding appears to be independent of adenylate nucleotide. High mole ratios of Smc2/4:plasmid promote a geometric change in circular DNA that can be trapped as knots by type II topoisomerases, but not as supercoils by a type I topoisomerase. Binding titration analyses reveal that two Smc2/4-DNA bound states exist: one disrupted by and one resistant to salt challenge. Competition-displacement experiments show that Smc2/4-DNA bound species formed at even high protein:DNA mole ratios remain reversible. Surprisingly, only linear and supercoiled DNA, not nicked-circular DNA, can completely displace Smc2/4 prebound to a labeled, nicked-circular DNA. In order to explain this geometry-dependent competition, we present two models of DNA binding by SMCs in which two DNA duplexes are captured within the inter-coil space of an Smc2/4 heterodimer. Based on these models, we propose a DNA displacement mechanism to explain how differences in geometry could affect the competitive potential of DNA.
J. Biol. Chem, 10.1074/jbc.M302699200
Submitted on March 17, 2003
Revised on April 23, 2003
Accepted on April 28, 2003
Biochemical analysis of the yeast condensin Smc2/4 complex: An ATPase that promotes knotting of circular DNA
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