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Inositol polyphosphate kinase activity of Arg82/ArgRIII is not required for the regulation of the arginine metabolism in yeast
Author(s) -
Dubois Evelyne,
Dewaste Valérie,
Erneux Christophe,
Messenguy Francine
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02318-8
Subject(s) - inositol , arginine , polyphosphate , kinase , regulator , biochemistry , arginine kinase , yeast , metabolism , inositol phosphate , biology , microbiology and biotechnology , chemistry , gene , receptor , phosphate , amino acid
Arg82, a nuclear regulator of diverse cellular processes in yeast, is an inositol polyphosphate kinase. Some defects such as the regulation of arginine metabolism observed in an arg82 Δ, result from a lack of Mcm1 and Arg80 stability. We show here that neither the kinase activity of Arg82 nor inositol phosphates are required for the control of arginine metabolism. Arg82 mutations keeping kinase active affect the expression of arginine genes, whereas mutations in the kinase domain do not impair this metabolic control.