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 Bioljournal_title
Molecular and cellular biologyauthors
Horiuchi H,Kaibuchi K,Kawamura M,Matsuura Y,Suzuki N,Kuroda Y,Kataoka T,Takai Ydoi
10.1128/mcb.12.10.4515subject
Has Abstractpub_date
1992-10-01 00:00:00pages
4515-20issue
10eissn
0270-7306issn
1098-5549journal_volume
12pub_type
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