tailieunhanh - Báo cáo Y học: Identification and characterization of the Escherichia coli stress protein UP12, a putative in vivo substrate of GroEL

Many groups of proteins play important roles in the cell’s response to various stresses. The molecular chaperone GroEL of Escherichia coli represents one such highly conserved family of stress proteins. We have observed that isolated GroEL complexes from stationary cultures contain various polypeptides that can be released from the chaperonin by GroES and/or ATP, and identified two such polypeptides as the proteins GatY and UP12. Whereas GatY had been isolated previously, as an in vivo substrate of GroEL, the isolation of UP12 in a complex with GroEL was intriguing, because based on sequence similarity it was suggested that UP12 might. | Eur. J. Biochem. 269 3032-3040 2002 FEBS 2002 doi Identification and characterization of the Escherichia coli stress protein UP12 a putative in vivo substrate of GroEL Elena S. Bochkareva Alexander S. Girshovich and Eitan Bibi Department of Biological Chemistry Weizmann Institute of Science Rehovot Israel Many groups of proteins play important roles in the cell s response to various stresses. The molecular chaperone GroEL of Escherichia coli represents one such highly conserved family of stress proteins. We have observed that isolated GroEL complexes from stationary cultures contain various polypeptides that can be released from the chaperonin by GroES and or ATP and identified two such polypeptides as the proteins GatY and UP12. Whereas GatY had been isolated previously as an in vivo substrate of GroEL the isolation of UP12 in a complex with GroEL was intriguing because based on sequence similarity it was suggested that UP12 might also be a functional stress protein. UP12 belongs to a family of universal stress proteins UspA family of which UspA itself and three additional paralogues have been characterized previously. Here we show that UP12 accumulates under various growth inhibitory conditions and induced by heat shock. Furthermore unlike wild-type cells a UP12 deletion mutant recovers slowly from late stationary growth conditions and has a marked sensitivity to the toxic agent carbonyl cyanide m-chlorophenyl hydrazone CCCP . Finally coimmunoprecipitation experiments confirmed the initial observation that UP12 interacts with GroEL. Therefore we suggest that UP12 may function as a universal stress protein interaction of which with GroEL possibly ensures its proper folding state. Keywords GroEL substrate UP12 universal stress protein Stress response E. ctl i. Escherichia coli cells undergo a transition from a rapid growth phase to a stationary phase which is accompanied by a variety of physiological changes that affect gene .

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