PHOSPHORYLATION AND DEPHOSPHORYLATION MODULATION OF AN INVERSE TEMPERATURE TRANSITION

被引:32
作者
PATTANAIK, A
GOWDA, DC
URRY, DW
机构
[1] Laboratory of Molecular Biophysics, School of Medicine The University of Alabama at Birmingham P. O., University Station, Birmingham, AL 35294-0019
关键词
D O I
10.1016/0006-291X(91)90141-S
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Poly[15(IPGVG),(RGYSLG)], where RGYSLG is a protein kinase site, was synthesized. On raising the temperature of a 5 mg/ml solution, this polypeptide undergoes an inverse temperature transition at 18°C in which it folds into a contracted state by optimizing intramolecular hydrophobic interactions. Averaging the data of five experiments, phosphorylation by means of a 3′:5′ cyclic AMP dependent protein kinase to the extent of one phosphate in 360 residues raises the temperature of the folding transition to 32°C. The shift is completely reversed on dephosphorylation by alkaline phosphatase. Phosphorylation is hereby shown to be the most potent chemical perturbation known for shifting the temperature of an inverse temperature transition, which has been shown to be an efficient mechanism for achieving chemomechanical transduction (mechanochemical coupling). © 1991.
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页码:539 / 545
页数:7
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