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Serine‐threonine protein kinase activity of Elm1p, a regulator of morphologic differentiation in Saccharomyces cerevisiae
Author(s) -
Koehler Carla M,
Myers Alan M
Publication year - 1997
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(97)00401-8
Subject(s) - autophosphorylation , saccharomyces cerevisiae , biochemistry , threonine , serine , akt3 , protein kinase a , biology , phosphorylation , map2k7 , kinase , protein phosphorylation , yeast , cyclin dependent kinase 2
The Saccharomyces cerevisiae gene ELM1 regulates morphologic differentiation and its nucleotide sequence predicts a novel protein kinase. Elm1p was expressed in yeast and insect cells and purified. Elm1p displayed protein kinase activity in autophosphorylation assays and towards exogenous substrates. Serine and threonine residues were identified as the acceptors in these reactions. These data together with previous genetic analysis of ELM1 function indicate that phosphorylation on serine and/or threonine residues of a particular substrate or set of substrates by Elm1p is required for repression of the filamentous growth differentiation state.