A COMMON PEPTIDE STRETCH AMONG ENZYMES LOCALIZED TO THE GOLGI-APPARATUS - STRUCTURAL SIMILARITY OF GOLGI-ASSOCIATED GLYCOSYLTRANSFERASES

被引：13

作者：

BENDIAK, B ^{[1
]}

机构：

[1] UNIV WASHINGTON,DEPT PATHOBIOL,SEATTLE,WA 98119

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 170卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)92173-W

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：

A common peptide motif has been discovered among a series of Golgi-localized glycosyltransferases. The peptide stretch, ( Ser Thr)-X-( Glu Gln)-( Arg Lys), always occurs near a hydrophobic domain close to the N-terminus of these enzymes which is believed to anchor them to the membrane lipid bilayer (Paulson and Colley, J. Biol. Chem., 264, 17615-17618, 1989). The finding that this similar peptide motif is not associated with catalytic activity of these enzymes, and its presence near the hydrophobic domain suggest that the stretch may be involved in localization of these enzymes to the Golgi apparatus. © 1990.

引用

页码：879 / 882

页数：4

共 17 条

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