THE ESSENTIAL YEAST NLT1 GENE ENCODES THE 64-KDA GLYCOPROTEIN SUBUNIT OF THE OLIGOSACCHARYL TRANSFERASE

被引：21

作者：

PATHAK, R ^{[1
]}

PARKER, CS ^{[1
]}

IMPERIALI, B ^{[1
]}

机构：

[1] CALTECH,DIV CHEM & CHEM ENGN,PASADENA,CA 91125

来源：

FEBS LETTERS | 1995年 / 362卷 / 02期

关键词：

OLIGOSACCHARYL TRANSFERASE; PROTEIN GLYCOSYLATION; ENDOPLASMIC RETICULUM; SACCHAROMYCES CEREVISIAE;

D O I：

10.1016/0014-5793(95)00253-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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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页码：229 / 234

页数：6

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