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Article

Mutations of Ha-ras p21 that define important regions for the molecular mechanism of the SDC25 C-domain, a guanine nucleotide dissociation stimulator.

The EMBO journal - 1 Jul 1992

Mistou M Y, Jacquet E, Poullet P, Rensland H, Gideon P, Schlichting I, Wittinghofer A, Parmeggiani A

Abstract excerpt

The SDC25 C-domain is a very active guanine nucleotide dissociation stimulator (GDS) isolated from Saccharomyces cerevisiae which acts equally well on Ha-ras p21 and yeast RAS2. These properties make the SDC25 C-domain a suitable tool to study the basic mechanism of a GDS. The action of the SDC25 C-domain was analysed by mutation of structurally important regions of p21. Substitutions that influence the...

Topics

Escherichia coli
Fungal Proteins
GTP-Binding Proteins
Genes, Bacterial
Guanine Nucleotides
Kinetics
Molecular Conformation
Mutation
Proto-Oncogene Proteins p21(ras)
Saccharomyces cerevisiae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

rap GTP-Binding Proteins

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Identifiers

PMID: 1628612
DOI: 10.1002/j.1460-2075.1992.tb05303.x
PMCID: PMC556713

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1628612-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Mutations of Ha-ras p21 that define important regions for the molecular mechanism of the SDC25 C-domain, a guanine nucleotide dissociation stimulator.PMID 1628612Read ↗

Properties of the SDC25 C-domain, a GDP to GTP exchange factor of RAS proteins and in vitro modulation of adenylyl cyclase.Semantic proximity Read ↗

RAS residues that are distant from the GDP binding site play a critical role in dissociation factor-stimulated release of GDP.Semantic proximity Read ↗

Biochemical characterization of C3G: an exchange factor that discriminates between Rap1 and Rap2 and is not inhibited by Rap1A(S17N).Semantic proximity Read ↗

SDC25, a dispensable Ras guanine nucleotide exchange factor of Saccharomyces cerevisiae differs from CDC25 by its regulation.Semantic proximity Read ↗

Structural requirements for the interaction of p21ras with GAP, exchange factors, and its biological effector target.Semantic proximity Read ↗

Interaction between the Saccharomyces cerevisiae CDC25 gene product and mammalian ras.Semantic proximity Read ↗

SDC25, a CDC25-like gene which contains a RAS-activating domain and is a dispensable gene of Saccharomyces cerevisiae.Semantic proximity Read ↗

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Dimerization of Cdc25p, the guanine-nucleotide exchange factor for Ras from Saccharomyces cerevisiae, and its interaction with Sdc25p.Semantic proximity Read ↗

p21 with a phenylalanine 28----leucine mutation reacts normally with the GTPase activating protein GAP but nevertheless has transforming properties.Semantic proximity Read ↗

Three-dimensional structure and properties of wild-type and mutant H-ras-encoded p21.Semantic proximity Read ↗

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