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Vol. 10, Issue 1, 63-75, January 1999
Department of Molecular Genetics, Max-Planck-Institut for
Biophysical Chemistry, D-37070 Göttingen, Germany
The yeast transport GTPase Ypt6p is dispensable for cell growth and
secretion, but its lack results in temperature sensitivity and
missorting of vacuolar carboxypeptidase Y. We previously identified four yeast genes (SYS1, 2, 3, and 5) that
on high expression suppressed these phenotypic alterations.
SYS3 encodes a 105-kDa protein with a predicted high
-helical content. It is related to a variety of mammalian
Golgi-associated proteins and to the yeast Uso1p, an essential protein
involved in docking of endoplasmic reticulum-derived vesicles to the
cis-Golgi. Like Uso1p, Sys3p is predominatly cytosolic. According to gel chromatographic, two-hybrid, and chemical
cross-linking analyses, Sys3p forms dimers and larger protein
complexes. Its loss of function results in partial missorting of
carboxypeptidase Y. Double disruptions of SYS3
and YPT6 lead to a significant growth inhibition of the
mutant cells, to a massive accumulation of 40- to 50-nm vesicles, to an
aggravation of vacuolar protein missorting, and to a defect in
-pheromone processing apparently attributable to a perturbation of
protease Kex2p cycling between the Golgi and a post-Golgi compartment.
The results of this study suggest that Sys3p, like Ypt6p, acts in
vesicular transport (presumably at a vesicle-docking stage) between an
endosomal compartment and the most distal Golgi compartment.
Corresponding author. E-mail address:
dgallwi1{at}gwdg.de.
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