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. 1994 Dec;14(12):8117–8122. doi: 10.1128/mcb.14.12.8117

Amino acid residues in the CDC25 guanine nucleotide exchange factor critical for interaction with Ras.

W Park 1, R D Mosteller 1, D Broek 1
PMCID: PMC359350  PMID: 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.

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Selected References

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