The posttranslational processing of ras p21 is critical for its stimulation of yeast adenylate cyclase.

Abstract:

:Mammalian ras genes substitute for the yeast RAS gene, and their products activate adenylate cyclase in yeast cells, although the direct target protein of mammalian ras p21s remains to be identified. ras p21s undergo posttranslational processing, including prenylation, proteolysis, methylation, and palmitoylation, at their C-terminal regions. We have previously reported that the posttranslational processing of Ki-ras p21 is essential for its interaction with one of its GDP/GTP exchange proteins named smg GDS. In this investigation, we have studied whether the posttranslational processing of Ki- and Ha-ras p21s is critical for their stimulation of yeast adenylate cyclase in a cell-free system. We show that the posttranslationally fully processed Ki- and Ha-ras p21s activate yeast adenylate cyclase far more effectively than do the unprocessed proteins. The previous and present results suggest that the posttranslational processing of ras p21s is important for their interaction not only with smg GDS but also with the target protein.

journal_name

Mol Cell Biol

authors

Horiuchi H,Kaibuchi K,Kawamura M,Matsuura Y,Suzuki N,Kuroda Y,Kataoka T,Takai Y

doi

10.1128/mcb.12.10.4515

subject

Has Abstract

pub_date

1992-10-01 00:00:00

pages

4515-20

issue

10

eissn

0270-7306

issn

1098-5549

journal_volume

12

pub_type

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