Title Physiological Relevance of Salt Environment for in vitro recA System
Author Kim, Jong Il
Address Major in Food and Microbial Technology, Faculty of Natural Sciences Seoul Women's University
Bibliography Journal of Microbiology, 37(2),59-65, 1999,
Key Words recA protein, DNA strand exchange, ATP hydrolysis, heterosuplex formation, in vivo salt environment
Abstract RecA protein can promote strand assimilation, homologous pairing, and strand exchange. All these reactions require DNA-dependent ATP hydrolysis by recA protein, and the activities of recA protein are affected by the ionic environment. In this experiment, DNA-dependent ATPase activity showed different sensitivity to anionic species. ATP hydrolysis and strand exchange were relatively sensitive to salt in the reactions with NaCl, strongly inhibited at 100 mM NaCl. However, the inhibition by sodium acetate or sodium glutamate was not observed at 50∼100 mM concentration. Addition of sodium glutamate to the standard reaction condition increased the apparent efficiency of ATP hydrolysis during strand exchange. The condition including 50∼100 mM sodium-glutamate might be similar to the physiological condition.
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