Conversion of the guanine nucleotide binding sites of ras protein resulting in the reduction of base specificity

K Miura; H Kamiya; S Kubota; M Ikehara; S Nishimura; E Ohtsuka

doi:10.1093/protein/2.3.227

Conversion of the guanine nucleotide binding sites of ras protein resulting in the reduction of base specificity

Protein Eng. 1988 Sep;2(3):227-31. doi: 10.1093/protein/2.3.227.

Authors

K Miura¹, H Kamiya, S Kubota, M Ikehara, S Nishimura, E Ohtsuka

Affiliation

¹ Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.

PMID: 3070545
DOI: 10.1093/protein/2.3.227

Abstract

A gene coding for the novel ras protein, p21X, in which the domains of guanine binding and phosphate binding were exchanged, was constructed and expressed in Escherichia coli. The gene product, p21X, showed GTP binding activity, but no GPTase activity. In addition, p21X revealed binding activity toward ATP and CTP. In a competitive binding assay, [3H]GTP binding to p21X was inhibited in the presence of ATP, CTP and UTP, ITP as well as GDP, GTP and dGTP.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Escherichia coli / genetics
GTP Phosphohydrolases / metabolism
Genes, ras*
Guanine Nucleotides / metabolism*
Humans
Models, Molecular
Molecular Sequence Data
Proto-Oncogene Proteins / isolation & purification
Proto-Oncogene Proteins / metabolism*
Proto-Oncogene Proteins p21(ras)
Substrate Specificity

Substances

Guanine Nucleotides
Proto-Oncogene Proteins
GTP Phosphohydrolases
HRAS protein, human
Proto-Oncogene Proteins p21(ras)