SERINE-THREONINE PROTEIN-KINASE ACTIVITY OF ELM1P, A REGULATOR OF MORPHOLOGIC DIFFERENTIATION IN SACCHAROMYCES-CEREVISIAE

Citation
Cm. Koehler et Am. Myers, SERINE-THREONINE PROTEIN-KINASE ACTIVITY OF ELM1P, A REGULATOR OF MORPHOLOGIC DIFFERENTIATION IN SACCHAROMYCES-CEREVISIAE, FEBS letters, 408(1), 1997, pp. 109-114
Citations number
27
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
408
Issue
1
Year of publication
1997
Pages
109 - 114
Database
ISI
SICI code
0014-5793(1997)408:1<109:SPAOEA>2.0.ZU;2-E
Abstract
The Saccharomyces cerevisiae gene ELM1 regulates morphologic different iation and its nucleotide sequence predicts a novel protein kinase. El m1p was expressed in yeast and insect cells and purified. Elm1p displa yed protein kinase activity in autophosphorylation assays and towards exogenous substrates. Serine and threonine residues were identified as the accepters in these reactions. These data together with previous g enetic analysis of ELM1 function indicate that phosphorylation on seri ne and/or threonine residues of a particular substrate or set of subst rates by Elm1p is required for repression of the filamentous growth di fferentiation state. (C) 1997 Federation of European Biochemical Socie ties.