Primary structure and biochemical characterization of yeast GTPase-activating proteins with substrate preference for the transport GTPase Ypt7p.

@article{Vollmer1999PrimarySA,
  title={Primary structure and biochemical characterization of yeast GTPase-activating proteins with substrate preference for the transport GTPase Ypt7p.},
  author={Petra Vollmer and Elke Will and Dietrich Scheglmann and Molly Strom and Dieter Gallwitz},
  journal={European journal of biochemistry},
  year={1999},
  volume={260 1},
  pages={284-90}
}
Small GTPases of the Ypt/Rab family are regulators of vesicular protein trafficking in exo-and endocytosis. GTPase-activating proteins (GAP) play an important role as down regulators of GTPases. We here report the molecular cloning of a novel GAP-encoding gene (GYP7, for GAP for Ypt7) by high expression from a Saccharomyces cerevisiae genomic library. The GYP7 gene encodes a hydrophilic protein with a molecular mass of 87 kDa. Comparison of its primary sequence with that of the three other… CONTINUE READING

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