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Gene Review:

OST4 - Ost4p

Saccharomyces cerevisiae S288c

Synonyms: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4, OTase 4 kDa subunit, Oligosaccharyl transferase 4 kDa subunit, Oligosaccharyl transferase subunit OST4, YDL232W

Kim, H. et al., Chi, J.H. et al., Kim, H. et al., Karaoglu, D. et al., Zubkov, S. et al.

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High impact information on OST4

The residues critical for the OT activity and the stability of Stt3p-Ost4p-Ost3p subcomplex are located in helix alpha2, the larger cytosolic half of this kinked helix [1].
To learn where this region of Ost4p is situated in relation to the faces of endoplasmic reticulum (ER) membrane, we determined the membrane topology of Ost4p using an in vivo method and established that it is an Nlumen-Ccyto, type I membrane protein [2].
Introduction of Lys or Asp residues at other positions in the putative transmembrane domain or at the N or C terminus of Ost4p had no effect on disrupting subunit interactions or impairing the activity of OT [3].
This analysis indicated that when single amino acid residues in a region close to the luminal face of the putative transmembrane domain of Ost4p were changed into an ionizable amino acid such as Lys or Asp, growth at 37 degrees C and OT activity measured in vitro were impaired [3].
Stt3p and Ost4p were previously identified in screens for gene products involved in N-linked glycosylation [4].

Biological context of OST4

The OST4 open reading frame is unusual in that it predicts a protein of only 36 amino acids [5].

Associations of OST4 with chemical compounds

Here we describe the phenotypic characterization of ost4, a vanadate-resistant mutant that is defective in oligosaccharyltransferase (OTase) activity both in vivo and in vitro [5].

Other interactions of OST4

The highly conserved Stt3 protein is a subunit of the yeast oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p [4].

Analytical, diagnostic and therapeutic context of OST4

In addition, using immunoprecipitation techniques and Western blot analysis, we found that with these mutations the interaction between Ost4p, Ost3p, and Stt3p was disrupted [3].

References

Structural basis for the function of a minimembrane protein subunit of yeast oligosaccharyltransferase. Zubkov, S., Lennarz, W.J., Mohanty, S. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
Determination of the membrane topology of Ost4p and its subunit interactions in the oligosaccharyltransferase complex in Saccharomyces cerevisiae. Kim, H., Yan, Q., Von Heijne, G., Caputo, G.A., Lennarz, W.J. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
Studies on the role of the hydrophobic domain of Ost4p in interactions with other subunits of yeast oligosaccharyl transferase. Kim, H., Park, H., Montalvo, L., Lennarz, W.J. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
The highly conserved Stt3 protein is a subunit of the yeast oligosaccharyltransferase and forms a subcomplex with Ost3p and Ost4p. Karaoglu, D., Kelleher, D.J., Gilmore, R. J. Biol. Chem. (1997) [Pubmed]
The OST4 gene of Saccharomyces cerevisiae encodes an unusually small protein required for normal levels of oligosaccharyltransferase activity. Chi, J.H., Roos, J., Dean, N. J. Biol. Chem. (1996) [Pubmed]

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