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Identification and partial purification of GTPase‐activating proteins from yeast and mammalian cells that preferentially act on Ypt1/Rab1 proteins
Author(s) -
Tan Tjie J.,
Vollmer Petra,
Gallwitz Dieter
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81312-v
Subject(s) - gtpase , yeast , effector , saccharomyces cerevisiae , cytosol , gtpase activating protein , biochemistry , microbiology and biotechnology , mutant , biology , chemistry , receptor , g protein , gene , enzyme
Two GTPase‐activating proteins of apparent molecular mass of 100 kDa and 30 kDa have been partially purified from porcine liver cytosol usinig mammalian Ypt1/Rab1 protein as substrate. Both proteins act most efficiently on Ypt1/Rab1 p, 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 Yptlp 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.