CLEAVAGE WITHOUT ANCHOR ADDITION ACCOMPANIES THE PROCESSING OF A NASCENT PROTEIN TO ITS GLYCOSYLPHOSPHATIDYLINOSITOL-ANCHORED FORM

被引：39

作者：

MAXWELL, SE ^{[1
]}

RAMALINGAM, S ^{[1
]}

GERBER, LD ^{[1
]}

UDENFRIEND, S ^{[1
]}

机构：

[1] ROCHE INST MOLEC BIOL,ROCHE RES CTR,NUTLEY,NJ 07110

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 05期

关键词：

ENDOPLASMIC RETICULUM; COOH-TERMINAL SIGNAL PEPTIDE; TRANSAMIDASE;

D O I：

10.1073/pnas.92.5.1550

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Rough microsomal membranes from most mammalian cells, in the presence of a translation system, process nascent proteins with appropriate COOH-terminal signal peptides to their mature glycosylphosphatidylinositol (GPI)-linked forms. The present study, using preprominiplacental alkaline phosphatase as substrate, shows that as much as 10% of the mature product is cleaved correctly but is not linked to GPI. Some of the factors that influence the relative proportions of GPI linked to free mini-placental alkaline phosphatase are the amounts of GPI in the cells and the amino acid substituent at the omega site of the nascent protein. A mechanism for explaining cleavage both with and without GPI addition is presented, which supports a transamidase type of enzyme as the catalyst.

引用

页码：1550 / 1554

页数：5

共 18 条

[1] EVIDENCE THAT THE PUTATIVE COOH-TERMINAL SIGNAL TRANSAMIDASE INVOLVED IN GLYCOSYLPHOSPHATIDYLINOSITOL PROTEIN-SYNTHESIS IS PRESENT IN THE ENDOPLASMIC-RETICULUM [J].