Comparative biochemical properties of normal and activated human ras p21 protein

Human Ha-ras1 cDNAs encoding normal and activated p21 polypeptides have been efficiently expressed in Escherichia coli and the biochemical activities associated with each polypeptide compared. In addition to the guanine nucleotide binding activity, normal p21 displays a GTPase activity which is sele...

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Bibliographic Details
Published inNature (London) Vol. 310; no. 5979; p. 644
Main Authors McGrath, J P, Capon, D J, Goeddel, D V, Levinson, A D
Format Journal Article
LanguageEnglish
Published England 01.08.1984
Subjects
Cloning, Molecular
DNA - metabolism
DNA Restriction Enzymes
Escherichia coli - genetics
GTP Phosphohydrolases - genetics
Guanosine Triphosphate - metabolism
Humans
Mutation
Neoplasm Proteins - genetics
Oncogene Protein p21(ras)
Oncogenes
Phosphorylation
Protein Binding
Proto-Oncogene Proteins p21(ras)
RNA, Messenger - genetics
Substrate Specificity
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Summary:Human Ha-ras1 cDNAs encoding normal and activated p21 polypeptides have been efficiently expressed in Escherichia coli and the biochemical activities associated with each polypeptide compared. In addition to the guanine nucleotide binding activity, normal p21 displays a GTPase activity which is selectively impaired by a mutation which activates its oncogenic potential.
ISSN:0028-0836
DOI:10.1038/310644a0