A mouse CDC25-like product enhances the formation of the active GTP complex of human ras p21 and Saccharomyces cerevisiae RAS2 proteins
作者： E Jacquet , M Vanoni , C Ferrari , L Alberghina , E Martegani
DOI: 10.1016/S0021-9258(18)35747-8
关键词: GTP' 、 Ras-GRF1 、 Ras2 、 G protein 、 Saccharomyces cerevisiae 、 Biochemistry 、 GTP-binding protein regulators 、 Biology 、 Proto-Oncogene Proteins p21(ras) 、 Rap GTP-binding protein
摘要: GDP-dissociation stimulators (GDSs) are the key element for regeneration of active state ras proteins, but despite intensive investigations, little is so far known about their functional and structural properties, particularly in mammals. A growing number genes from various organisms have been postulated to encode GDSs on basis sequence similarity with Saccharomyces cerevisiae CDC25 gene, whose product acts as a GDS RAS proteins. However, except related SDC25 C-domain, no biochemical evidence activity these CDC25-like proteins has yet available. We show that recently isolated mouse gene (CDC25Mm) can strongly enhance (more than 1000 times) GDP release both human c-Ha-ras p21 yeast RAS2 vitro. As consequence, CDC25Mm induces rapid formation biologically Ras.GTP complex. This much more GTP complex narrow substrate specificity, since it was found be inactive several ras-like The efficiently substitute an vitro adenylylcyclase assay cdc25 membranes. Our results cloned exchange factor mammalian belongs novel family
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