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J Biol Chem, Vol. 274, Issue 24, 17249-17256, June 11, 1999
From the Lehrstuhl für Zellbiologie und Pflanzenphysiologie,
Universität Regensburg, Universitätsstrasse 31, 93053 Regensburg, Germany
The key step of N-glycosylation of
proteins, an essential and highly conserved protein modification, is
catalyzed by the hetero-oligomeric protein complex
oligosaccharyltransferase (OST). So far, eight genes have been
identified in Saccharomyces cerevisiae that are involved in
this process. Enzymatically active OST preparations from yeast were
shown to be composed of four (Ost1p, Wbp1p, Ost3p, Swp1p) or six
subunits (Ost2p and Ost5p in addition to the four listed). Genetic
studies have disclosed Stt3p and Ost4p as additional proteins needed
for N-glycosylation. In this study we report the identification and functional characterization of a new OST gene, designated OST6, that has homology to OST3 and
in particular a strikingly similar membrane topology. Neither gene is
essential for growth of yeast. Disruption of OST6 or
OST3 causes only a minor defect in
N-glycosylation, but an 
ost3ost6
double mutant displays a synthetic phenotype, leading to a
severe underglycosylation of soluble and membrane-bound glycoproteins
in vivo and to a reduced OST activity in vitro.
Moreover, each of the two genes has also a specific function, since
agents affecting cell wall biogenesis reveal different growth
phenotypes in the respective null mutants. By blue native
electrophoresis and immunodetection, a ~240-kDa complex was
identified consisting of Ost1p, Stt3p, Wbp1p, Ost3p, Ost6p, Swp1p,
Ost2p, and Ost5p, indicating that probably all so far identified OST
proteins are constituents of the OST complex. It is also shown
that disruption of OST3 and OST6 leads to a
defect in the assembly of the complex. Hence, the function of these
genes seems to be essential for recruiting a fully active complex
necessary for efficient N-glycosylation.
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