In:
FEBS Letters, Wiley, Vol. 255, No. 1 ( 1989-09-11), p. 139-142
Abstract:
The relationship between protein glycosylation and fatty acylation of glycoproteins was studied in the wild‐type and asparagine‐linked glycosylation‐deficient mutants ( alg1 and alg2 ) of Saccharomyces cerevisiae . At the non‐permissive temperature (37°C), both mutant cells exhibited increased incorporation of [ 3 H]palmitate into five polypeptides based on SDS‐PAGE. In contrast, the wild‐type yeast cells contained [ 3 H]palmitate‐labeled polypeptides of higher molecular weights, which were converted to the bands seen in the mutant cells upon treatment of the cell extract with endoglycosidase H prior to SDS‐PAGE. In addition, labeling of the wild‐type yeast cells with [ 3 H]palmitate in the presence of tunicamycin revealed the incorporation of [ 3 H]palmitate into the same five bands as found in the alg1 and alg2 mutants at the non‐permissive temperature without tunicamycin. These results indicate that fatty acylation of glycoproteins proceeds independently of protein N ‐glycosylation in yeast cells.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(89)81077-4
Language:
English
Publisher:
Wiley
Publication Date:
1989
detail.hit.zdb_id:
1460391-3
SSG:
12
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