CHARACTERIZATION OF AN ACYLTRANSFERASE ACTING ON P21N-RAS PROTEIN IN A CELL-FREE SYSTEM

被引：64

作者：

GUTIERREZ, L ^{[1
]}

MAGEE, AI ^{[1
]}

机构：

[1] NATL INST MED RES,MILL HILL,LONDON NW7 1AA,ENGLAND

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1991年 / 1078卷 / 02期

关键词：

PROTEIN P21RAS; ACYLTRANSFERASE; CELL-FREE SYSTEM;

D O I：

10.1016/0167-4838(91)99003-B

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：

We have identified a protein-acyltransferase activity in membranes from mouse fibroblasts which transfers palmitate from palmitoyl-CoA to p21N-ras. Specificity of acylation has been confirmed by linkage analysis using hydroxylamine and by peptide mapping of in vivo and in vitro acylated p21N-ras. The acylation was temperature- and time-dependent, and prevented by prior boiling of membranes, consistent with an enzymatic process. The activity was detected in membranes, but not cytosol, and co-fractionated on Percoll gradients with Golgi markers. Cytosolic p21N-ras from mouse fibroblasts, which is C-terminally modified at its CAAX sequence, was a better substrate for the enzyme than recombinant bacterially expressed, unmodified p21N-ras. The activity could be solubilised in non-ionic detergents, making it amenable to purification.

引用

页码：147 / 154

页数：8

共 51 条

[31] CHARACTERIZATION OF A MANNOSIDASE ACTING ON ALPHA-1-]3-LINKED AND ALPHA-1-]6-LINKED MANNOSE RESIDUES OF OLIGOMANNOSIDIC INTERMEDIATES OF GLYCOPROTEIN PROCESSING [J].