Inhibition of SDC25 C-domain-induced guanine-nucleotide exchange by guanine ring binding domain mutants of v-H-ras.
作者： Y W Hwang , J M Zhong , P Poullet , A Parmeggiani
DOI: 10.1016/S0021-9258(19)74521-9
关键词:
摘要: Guanine-nucleotide exchange is the reaction that controls activation of H-ras p21. This stimulated by guanine-nucleotide factor. In this study we show p21 harboring guanine ring binding domain (the conserved NKXD motif) mutations, such as N116I or K117E, are potent inhibitors promoted SDC25C (Saccharomyces cerevisiae SDC25 C-domain gene product), a The inhibition due to formation stable but catalytically inactive complex consisting mutant and SDC25C. By examining interaction v-H-ras(N116I) v-H-ras(K117E) with at different concentrations guanine-nucleotide, demonstrate mechanism SDC25C-promoted proceeds through following pathway. First, binds forms an intermediate H-ras.SDC25C complex; subsequently, incoming dissociates complex, releasing from causes exchange. similar one proposed for Escherichia coli elongation factor Ts-catalyzed
sci-hub.st 参考文章(48)
E. Martegani, M. Vanoni, R. Zippel, P. Coccetti, R. Brambilla, C. Ferrari, E. Sturani, L. Alberghina, Cloning by functional complementation of a mouse cDNA encoding a homologue of CDC25, a Saccharomyces cerevisiae RAS activator. The EMBO Journal. ,vol. 11, pp. 2151- 2157 ,(1992) , 10.1002/J.1460-2075.1992.TB05274.X
H. Cen, A.G. Papageorge, R. Zippel, D.R. Lowy, K. Zhang, Isolation of multiple mouse cDNAs with coding homology to Saccharomyces cerevisiae CDC25: identification of a region related to Bcr, Vav, Dbl and CDC24. The EMBO Journal. ,vol. 11, pp. 4007- 4015 ,(1992) , 10.1002/J.1460-2075.1992.TB05494.X
N. C. Walworth, B. Goud, A. K. Kabcenell, P. J. Novick, Mutational analysis of SEC4 suggests a cyclical mechanism for the regulation of vesicular traffic. The EMBO Journal. ,vol. 8, pp. 1685- 1693 ,(1989) , 10.1002/J.1460-2075.1989.TB03560.X
Y.W. Hwang, M Carter, D.L. Miller, The identification of a domain in Escherichia coli elongation factor Tu that interacts with elongation factor Ts. Journal of Biological Chemistry. ,vol. 267, pp. 22198- 22205 ,(1992) , 10.1016/S0021-9258(18)41654-7
A Hall, A J Self, The effect of Mg2+ on the guanine nucleotide exchange rate of p21N-ras. Journal of Biological Chemistry. ,vol. 261, pp. 10963- 10965 ,(1986) , 10.1016/S0021-9258(18)67333-8
Y W Hwang, D L Miller, A study of the kinetic mechanism of elongation factor Ts. Journal of Biological Chemistry. ,vol. 260, pp. 11498- 11502 ,(1985) , 10.1016/S0021-9258(17)39057-9
Y W Hwang, A Sanchez, D L Miller, Mutagenesis of bacterial elongation factor Tu at lysine 136. A conserved amino acid in GTP regulatory proteins. Journal of Biological Chemistry. ,vol. 264, pp. 8304- 8309 ,(1989) , 10.1016/S0021-9258(18)83183-0
A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein. Journal of Biological Chemistry. ,vol. 262, pp. 13081- 13085 ,(1987) , 10.1016/S0021-9258(18)45170-8
E Jacquet, M Vanoni, C Ferrari, L Alberghina, E Martegani, A Parmeggiani, A mouse CDC25-like product enhances the formation of the active GTP complex of human ras p21 and Saccharomyces cerevisiae RAS2 proteins Journal of Biological Chemistry. ,vol. 267, pp. 24181- 24183 ,(1992) , 10.1016/S0021-9258(18)35747-8
C.F. Albright, B.W. Giddings, J. Liu, M. Vito, R.A. Weinberg, Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPase. The EMBO Journal. ,vol. 12, pp. 339- 347 ,(1993) , 10.1002/J.1460-2075.1993.TB05662.X