Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Serine-threonine protein kinase activity of Elm1p, a regulator of morphologic differentiation in Saccharomyces cerevisiae.

FEBS letters | May 12, 1997

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.

Pubmed ID: 9180279 RIS Download

Mesh terms: Blotting, Northern | Cell Division | Gene Expression Regulation, Fungal | Genes, Fungal | Microscopy, Phase-Contrast | Mutation | Phosphorylation | Phosphoserine | Phosphothreonine | Protein-Serine-Threonine Kinases | RNA, Messenger | Recombinant Fusion Proteins | Saccharomyces cerevisiae | Substrate Specificity

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

We have not found any resources mentioned in this publication.