Characterization of domains in the yeast MAP kinase Slt2 (Mpk1) required for functional activity and in vivo interaction with protein kinases Mkk1 and Mkk2

Molecular Microbiology
M SolerC Nombela

Abstract

MKK1/MKK2 and SLT2 (MPK1) are three Saccharomyces cerevisiae genes, coding for protein kinases, that have been postulated to act sequentially as part of the Pkc1p signalling pathway, a phosphorylation cascade essential for cell integrity. By using the 'two-hybrid system' and co-purification experiments on glutathione-agarose beads, we have shown that Slt2p interacts in vivo and in vitro with both Mkk1p and Mkk2p, thus confirming a previous suggestion based on epistasis experiments of the corresponding genes. Plasmid constructs of the SLT2 gene, deleted in the whole C-terminal non-kinase region or part of it, and therefore containing all of the conserved kinase subdomains, were still functional in complementation of the slt2 lytic phenotype and in vivo interaction with Mkk1p and Mkk2p. In contrast, the Slt2p C-terminal domain (162 residues) that carries a glutamine-rich fragment followed by a 16 polyglutamine tract, was shown to be dispensable for complementation and in vivo association with Mkk1p and Mkk2p. We have also demonstrated that the N-terminal putative regulatory domain of these two MAP kinase activators is the main region involved in the interaction with Slt2p.

Citations

Nov 26, 2009·FEMS Yeast Research·Bárbara Martínez-BonoJuan Carlos Igual
Jun 1, 2002·Microbiology and Molecular Biology Reviews : MMBR·Stefan Hohmann
Jun 10, 2005·Microbiology and Molecular Biology Reviews : MMBR·David E Levin
Apr 26, 2012·Molecular Systems Biology·Carl-Fredrik TigerMarcus Krantz
Aug 23, 2007·The Journal of Biological Chemistry·María Jiménez-SánchezMaría Molina
Dec 5, 1998·Microbiology and Molecular Biology Reviews : MMBR·M C GustinK Davenport

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