A UBIQUITYL-CALMODULIN SYNTHETASE THAT EFFECTIVELY RECOGNIZES THE CA-2+-FREE FORM OF CALMODULIN

被引:10
作者
MAJETSCHAK, M [1 ]
LAUB, M [1 ]
JENNISSEN, HP [1 ]
机构
[1] UNIV ESSEN GESAMTHSCH,INST PHYSIOL CHEM,HUFELANDSTR 55,W-4300 ESSEN 1,GERMANY
关键词
CALMODULIN; UBIQUITIN; UBIQUITYL-CALMODULIN SYNTHETASE; PROTEIN UBIQUITINATION; CALCIUM;
D O I
10.1016/0014-5793(93)81192-3
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
Ubiquityl-calmodulin synthetase (uCaM-synthetase) activity as detected in reticulocyte lysate and the crude extracts of rabbit tissues [FEBS Lett. 294 (1991) 229-2331 has been well characterized as being essentially Ca2+-dependent (-Ca2+/+Ca2+ activity ratio: 0.15-0.2). However, during the purification of this enzyme on ubiquitin-Sepharose the Ca2+-dependent activity is lost and an essentially Ca2+-independent enzyme (-Ca2+/+Ca2+ activity ratio: 1.0-1.5) is obtained which was purified 90-fold (uCaM-Syn F1) to a final specific activity of 0.32 pkat/mg. During the purification procedure a second protein factor (uCaM-Syn F2) was isolated that has no catalytic activity by itself but restores Ca2+ dependence to the uCaM-Syn F1 fraction (-Ca2+/+Ca2+ activity ratio: 0.1) and enhances the catalytic activity in uCaM-Syn F1 in the presence of Ca2+ over 40-fold. It is concluded that several (possibly interdependent) forms of uCaM-synthetase exist which display different substrate specificities for calmodulin.
引用
收藏
页码:347 / 352
页数:6
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