MUTANTS OF SACCHAROMYCES-CEREVISIAE DEFECTIVE IN THE FARNESYLATION OF RAS PROTEINS

被引：111

作者：

GOODMAN, LE

JUDD, SR

FARNSWORTH, CC

POWERS, S

GELB, MH

GLOMSET, JA

TAMANOI, F

机构：

[1] UNIV CHICAGO,DEPT BIOCHEM & MOLEC BIOL,920 E 58TH ST,CHICAGO,IL 60637

[2] UNIV WASHINGTON,HOWARD HUGHES MED INST LAB,SEATTLE,WA 98195

[3] UNIV WASHINGTON,DEPT MED & BIOCHEM,SEATTLE,WA 98195

[4] UNIV WASHINGTON,DEPT BIOCHEM,SEATTLE,WA 98195

[5] UNIV WASHINGTON,DEPT CHEM,SEATTLE,WA 98195

[6] UNIV MED & DENT NEW JERSEY,ROBERT WOOD JOHNSON MED SCH,DEPT BIOCHEM,PISCATAWAY,NJ 08854

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1990年 / 87卷 / 24期

关键词：

CAAX" box; C-terminal processing; Farnesyltransferase;

D O I：

10.1073/pnas.87.24.9665

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：

Ras proteins are post-translationally modified by farnesylation. In the present investigation, we identified an activity in crude soluble extracts of yeast cells that catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to yeast RAS2 protein. RAS2 proteins having a C-terminal Cys-Ali-Ali-Xaa sequence (where Ali is an aliphatic amino acid and Xaa is the unspecified C-terminal amino acid) served as substrates for this reaction, whereas RAS2 proteins with an altered or deleted Cys-Ali-Ali-Xaa sequence did not. A yeast mutant, dpr1/ram1, originally isolated as a Ras-processing mutant was shown to be defective in farnesyltransferase activity. In addition, another mutant, ram2, also was defective in the transferase activity. These results demonstrate that at least two genes, DPR1/RAM1 and RAM2, are required for the farnesyltransferase activity in yeast. (.

引用

页码：9665 / 9669

页数：5

共 26 条

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