TEHEESEN, S and LEHLE, L and WEISSMANN, A and AEBI, M (1994) ISOLATION OF THE ALG5 LOCUS ENCODING THE UDP-GLUCOSE-DOLICHYL-PHOSPHATE GLUCOSYLTRANSFERASE FROM SACCHAROMYCES-CEREVISIAE. EUROPEAN JOURNAL OF BIOCHEMISTRY, 224 (1). pp. 71-79. ISSN 0014-2956,
Full text not available from this repository.Abstract
UDP-glucose:dolichyl-phosphate glucosyltransferase is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. The structural gene encoding this transferase from Saccharomyces cerevisiae was isolated by complementation of an alg5-1 mutation. DNA sequencing of ALG5 revealed an open-reading frame of 1002 bases encoding a transmembrane protein of molecular mass 38.3 kDa. Overexpression of Alg5p in both yeast and Escherichia coli results in an increase of UDP-glucose:dolichyl-phosphate glucosyltransferase activity, whereas a deletion of the yeast gene leads to a loss of this activity and a concomitant underglycosylation of carboxypeptidase Y. The ALG5 protein has sequence similarity to the GDP-mannose: dolichylphosphate mannosyltransferase (Dpm1p) from S. cerevisiae. Topological studies indicate that UDP-glucose:dolichyl-phosphate glucosyltransferase is a transmembrane protein that spans the membrane several times.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MANNOSE SYNTHASE; GLYCOPROTEIN-BIOSYNTHESIS; OLIGOSACCHARIDE PRECURSOR; ENDOPLASMIC-RETICULUM; PROTEIN GLYCOSYLATION; MEMBRANE-PROTEIN; YEAST; GLYCOSYLTRANSFERASES; GLUCOSYLATION; RECOGNITION; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:40 |
| URI: | https://pred.uni-regensburg.de/id/eprint/53143 |
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