ArticleProceedings of the National Academy of Sciences of the United States of America2003
Determination of the membrane topology of Ost4p and its subunit interactions in the oligosaccharyltransferase complex in Saccharomyces cerevisiae.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 51 citations in OpenAlex.
- ReLo is a simple and rapid colocalization assay to identify and characterize direct protein-protein interactions.Nature communications · 2024Article
- Structural Insight into the Mechanism ofBiomolecules · 2020Review
- The topology of the ER-resident phospholipid methyltransferase Opi3 ofThe Journal of biological chemistry · 2020Article
- Chemical crosslinking and mass spectrometry to elucidate the topology of integral membrane proteins.PloS one · 2017Article
- Plant protein glycosylation.Glycobiology · 2016Review
- Topology of the yeast Ras converting enzyme as inferred from cysteine accessibility studies.Biochemistry · 2013Article
- OST4 is a subunit of the mammalian oligosaccharyltransferase required for efficient N-glycosylation.Journal of cell science · 2013Article
- Specialized roles of the conserved subunit OST3/6 of the oligosaccharyltransferase complex in innate immunity and tolerance to abiotic stresses.Plant physiology · 2013Article
- Review
- A novel and simple method of production and biophysical characterization of a mini-membrane protein, Ost4p: a subunit of yeast oligosaccharyl transferase.Biopolymers · 2012Article
- Topology of 1-acyl-sn-glycerol-3-phosphate acyltransferases SLC1 and ALE1 and related membrane-bound O-acyltransferases (MBOATs) of Saccharomyces cerevisiae.The Journal of biological chemistry · 2011Article
- Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation.Journal of inherited metabolic disease · 2011Review
- TIM23-mediated insertion of transmembrane α-helices into the mitochondrial inner membrane.The EMBO journal · 2011Article
- C terminus of Nce102 determines the structure and function of microdomains in the Saccharomyces cerevisiae plasma membrane.Eukaryotic cell · 2010Article
- Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional alpha1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis.The Journal of biological chemistry · 2009Article
- Article
- A global topology map of the Saccharomyces cerevisiae membrane proteome.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Dimeric organization of the yeast oligosaccharyl transferase complex.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Gpi19, the Saccharomyces cerevisiae homologue of mammalian PIG-P, is a subunit of the initial enzyme for glycosylphosphatidylinositol anchor biosynthesis.Eukaryotic cell · 2005Article
- Studies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: topological features and in vivo interactions.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Ost4p is a minimembrane protein containing only 36 amino acids and is a subunit of oligosaccharyltransferase (OT) in Saccharomyces cerevisiae. It was found previously when amino acid residues 18-25 of Ost4p were mutated to ionizable amino acids and defects were observed in the interaction between Ost4p and either Stt3p or Ost3p, two other components of OT. The transmembrane segment of Ost4p is likely to extend from residues 10-25. This is consistent with the finding that alpha-helicity is estimated to be 36% by CD analysis of synthetic Ost4p in liposomes. This value is in reasonable agreement with the assumption that amino acids 10-25 (16 of 36 or 44%) are transmembrane. Therefore, the mutation-sensitive region (residues 18-25) is localized to only one half of the putative transmembrane domain of Ost4p. 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. These results indicate that the mutation-sensitive region of Ost4p is localized in the cytoplasmic leaflet of the ER membrane. In the current study, we also observed a loss of direct interaction between Ost3p and Stt3p in the presence of ost4 temperature-sensitive mutants, which indicates Ost4p, via interactions with amino acid residues in the cytosolic leaflet of the ER membrane, functions to bind these two proteins together in a subcomplex of OT.
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