The essential yeastNLT1gene encodes the 64 kDa glycoprotein subunit of the oligosaccharyl transferase
In: FEBS Letters, Jg. 362 (1995-04-03), S. 229-234
Online
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Zugriff:
The yeast oligosaccharyl transferase catalyzes the glycosylation of asparagine residues in secreted, vesicular, and membrane proteins. A complex of at least four membrane-bound polypeptides is responsible for oligosaccharyl transferase activity. Amino acid sequences from the 64 kDa glycoprotein subunit of the complex were used to clone the essential NLT1 (N-linked oligosaccharyl transferase) gene. The Nlt1p gene product is a processed, multiply glycosylated type I membrane protein; it has an extensive amino-terminal soluble domain, a potential hydrophobic transmembrane domain, and a short carboxy-terminal soluble domain. The Nlt1p is significantly similar than the mammalian ribophorin I, a component of the mammalian oligosaccharyl transferase complex, and the enzyme is conserved throughout eukaryotic evolution.
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The essential yeastNLT1gene encodes the 64 kDa glycoprotein subunit of the oligosaccharyl transferase
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Autor/in / Beteiligte Person: | Imperiali, Barbara ; Pathak, Rahul ; Parker, Carl S. |
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Zeitschrift: | FEBS Letters, Jg. 362 (1995-04-03), S. 229-234 |
Veröffentlichung: | Wiley, 1995 |
Medientyp: | unknown |
ISSN: | 0014-5793 (print) |
DOI: | 10.1016/0014-5793(95)00253-6 |
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