Geeta Devgan

TL;DR: The in vitro substrates recognized by most yeast protein kinases are described, with the use of proteome chip technology, and these results will provide insights into the mechanisms and roles of protein phosphorylation in many eukaryotes.

TL;DR: In this article, the in vitro substrates recognized by most yeast protein kinases were identified, including closely related kinases of the protein kinase A family and four cyclin-dependent kinases that vary only in their cyclin subunits.

TL;DR: It is determined by peptide library selection and phosphosite array screening that the protein kinase Dbf2-Mob1 preferentially phosphorylated substrates that contain an RXXS motif, and a subsequent proteome microarray screen revealed proteins that can be phosphorylation by Dbf1 in vitro.

TL;DR: It is reported that Rim15 coordinates transcription with posttranscriptional mRNA protection by phosphorylating the paralogous Igo1 and Igo2 proteins, which shelters newly expressed mRNAs from degradation via the 5'-3' mRNA decay pathway, thereby enabling their proper translation during initiation of the G(0) program.

TL;DR: The construction and use of protein microarrays and their applications are described using yeast as a model system to reveal new activities of well-characterized proteins, thus providing new insights about the functions of these proteins.