Conversion of the guanine nucleotide binding sites of ras protein resulting in the reduction of base specificity.
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.
Miura
K
K
Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Kamiya
H
H
Kubota
S
S
Ikehara
M
M
Nishimura
S
S
Ohtsuka
E
E
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000235:genetics; D020558:GTP Phosphohydrolases / Q000378:metabolism; D011905:Genes, ras; D006150:Guanine Nucleotides / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011518:Proto-Oncogene Proteins / Q000302:isolation & purification / Q000378:metabolism*; D016283:Proto-Oncogene Proteins p21(ras); D013379:Substrate Specificity
D006150:Guanine Nucleotides; D011518:Proto-Oncogene Proteins; D020558:GTP Phosphohydrolases; C501009:HRAS protein, human; D016283:Proto-Oncogene Proteins p21(ras)