IDENTIFICATION AND PARTIAL-PURIFICATION OF GTPASE-ACTIVATING PROTEINS FROM YEAST AND MAMMALIAN-CELLS THAT PREFERENTIALLY ACT ON YPT1/RAB1 PROTEINS

被引：18

作者：

TAN, TJ ^{[1
]}

VOLLMER, P ^{[1
]}

GALLWITZ, D ^{[1
]}

机构：

[1] MAX PLANCK INST BIOPHYS CHEM,DEPT MOLEC GENET,POB 2841,W-3400 GOTTINGEN,GERMANY

来源：

FEBS LETTERS | 1991年 / 291卷 / 02期

关键词：

GTPASE-ACTIVATING PROTEIN; RAB1; PROTEIN; YPT1; PORCINE LIVER; SACCHAROMYCES-CEREVISIAE;

D O I：

10.1016/0014-5793(91)81312-V

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：

Two GTPase-activating proteins of apparent molecular mass of 100 kDa and 30 kDa have been partially purified from porcine liver cytosol using mammalian Ypt1/Rab1 protein as substrate. Both proteins act most efficiently on Ypt1/Rab1p, but are inactive with H-Ras p21. From the budding yeast Saccharomyces cerevisiae, a cytosolic 40 kDa yptGAP was partially purified. It accelerates the intrinsic GTPase activity of wild-type Ypt1p but not of H-Ras p21 or a mutant ypt1p with an animo acid substitution of the effector domain which renders the protein functionally inactive in yeast cells.

引用

页码：322 / 326

页数：5

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