Amino acid residues in the CDC25 guanine nucleotide exchange factor critical for interaction with Ras.
Mol Cell Biol
; 14(12): 8117-22, 1994 Dec.
Article
em En
| MEDLINE
| ID: mdl-7969149
ABSTRACT
Previously we found that negatively charged residues at positions 62, 63, and 69 of H-Ras are involved in binding to the CDC25 guanine nucleotide exchange factor (GEF). Using site-directed mutagenesis, we have changed conserved, positively charged residues of CDC25GEF to glutamic acid. We find the nonfunctional CDC25R1374E mutant and the nonfunctional H-RasE63K mutant cooperate in suppression of the loss of CDC25 function in Saccharomyces cerevisiae. Also, peptides corresponding to residues 1364 to 1383 of CDC25GEF inhibit interaction between GEFs and H-Ras. We propose that residues 1374 of CDC25GEF and 63 of H-Ras form an ion pair and that when this ion pair is reversed, functional interaction can still occur.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Proteínas Proto-Oncogênicas p21(ras)
/
Fosfoproteínas Fosfatases
Limite:
Humans
Idioma:
En
Ano de publicação:
1994
Tipo de documento:
Article