Comparative biochemical properties of normal and activated human ras p21 protein

Human Ha- ras 1 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 se...

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Bibliographic Details
Published in:Nature (London) 1984-08, Vol.310 (5979), p.644-649
Main Authors: McGrath, John P, Capon, Daniel J, Goeddel, David V, Levinson, Arthur D
Format: Article
Language:English
Subjects:
Biological and medical sciences
Cell physiology
Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes
Cloning, Molecular
DNA - metabolism
DNA Restriction Enzymes
Escherichia coli - genetics
Fundamental and applied biological sciences. Psychology
GTP Phosphohydrolases - genetics
Guanosine Triphosphate - metabolism
Humanities and Social Sciences
Humans
Molecular and cellular biology
multidisciplinary
Mutation
Neoplasm Proteins - genetics
Oncogene Protein p21(ras)
Oncogenes
Phosphorylation
Protein Binding
Proto-Oncogene Proteins p21(ras)
RNA, Messenger - genetics
Science
Science (multidisciplinary)
Substrate Specificity
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Summary:Human Ha- ras 1 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
1476-4687
DOI:10.1038/310644a0