Identification and partial purification of GTPase‐activating proteins from yeast and mammalian cells that preferentially act on Ypt1/Rab1 proteins
- 21 October 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 291 (2), 322-326
- https://doi.org/10.1016/0014-5793(91)81312-v
Abstract
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.Keywords
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