PEPTIDYL-PROLYL CIS-TRANS ISOMERASE IMPROVES THE EFFICIENCY OF PROTEIN DISULFIDE ISOMERASE AS A CATALYST OF PROTEIN FOLDING

被引:94
作者
SCHONBRUNNER, ER [1 ]
SCHMID, FX [1 ]
机构
[1] UNIV BAYREUTH,BIOCHEM LAB,W-8580 BAYREUTH,GERMANY
关键词
OXIDATIVE FOLDING; CYCLOPHILIN; RIBONUCLEASE-T1;
D O I
10.1073/pnas.89.10.4510
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The cis-trans isomerization of prolyl peptide bonds and the formation of disulfide bonds are both slow steps in protein folding. By using ribonuclease T1 as a model system, we show that these two processes can become linked in the oxidative folding of reduced proteins and that the formation of the correct disulfide bonds is facilitated in the presence of peptidyl-prolyl cis-trans isomerase. In particular, the efficiency of protein disulfide isomerase (EC 5.3.4.1) as a catalyst of disulfide bond formation in the course of oxidative folding is markedly improved when peptidyl-prolyl cis-trans isomerase is present simultaneously. Possibly, unfolded or partially folded protein chains with correct prolyl isomers are better substrates for catalysis by protein disulfide isomerase. The interdependence of the two enzymatic activities detected during in vitro folding experiments could be of importance for the de novo folding and disulfide bond formation of nascent proteins in the endoplasmic reticulum.
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页码:4510 / 4513
页数:4
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