ArticleEukaryotic cell2003
Ssk1p response regulator binding surface on histidine-containing phosphotransfer protein Ypd1p.
Article in Eukaryotic cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Role of the highly conserved G68 residue in the yeast phosphorelay protein Ypd1: implications for interactions between histidine phosphotransfer (HPt) and response regulator proteins.BMC biochemistry · 2019Article
- The phosphorelay signal transduction system in Candida glabrata: an in silico analysis.Journal of molecular modeling · 2017Article
- Histidine phosphotransfer proteins in fungal two-component signal transduction pathways.Eukaryotic cell · 2013Review
- Article
- Response to hyperosmotic stress.Genetics · 2012Review
- Multiple roles of Ypd1 phosphotransfer protein in viability, stress response, and virulence factor regulation in Cryptococcus neoformans.Eukaryotic cell · 2011Article
- Kinetic studies of the yeast His-Asp phosphorelay signaling pathway.Methods in enzymology · 2010Article
- Crystal structure of histidine phosphotransfer protein ShpA, an essential regulator of stalk biogenesis in Caulobacter crescentus.Journal of molecular biology · 2009Article
- Phosphorylated Ssk1 prevents unphosphorylated Ssk1 from activating the Ssk2 mitogen-activated protein kinase kinase kinase in the yeast high-osmolarity glycerol osmoregulatory pathway.Molecular and cellular biology · 2008Article
- Transcriptional profiling of the Candida albicans Ssk1p receiver domain point mutants and their virulence.FEMS yeast research · 2008Article
- Comparative analysis of HOG pathway proteins to generate hypotheses for functional analysis.Current genetics · 2006Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Ypd1p, a histidine-containing phosphotransfer protein, plays an important role in a branched His-Asp phosphorelay signal transduction pathway that regulates cellular responses to hyperosmotic stress in Saccharomyces cerevisiae. Ypd1p is required for phosphoryl group transfer from the membrane-bound Sln1p sensor histidine kinase to two downstream response regulator proteins, Ssk1p and Skn7p. To investigate the molecular basis for interaction of Ypd1p with these response regulator domains, we used an approach that coupled alanine-scanning mutagenesis of surface-exposed residues in Ypd1p with a yeast two-hybrid interaction screen. Mutated residues that adversely affected the interaction of Ypd1p with the C-terminal response regulator domain of Ssk1p were identified and found to cluster on or near the alphaA helix in Ypd1p. Our results, supported by analysis of a modeled complex, identify a binding site on Ypd1p for response regulators that is composed of a cluster of conserved hydrophobic residues surrounded by less conserved polar residues. We propose that molecular interactions involving Ypd1p are mediated primarily through hydrophobic contacts, whereas binding specificity and strength of interaction may be influenced by select polar side chain interactions.
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