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Structurally unique interaction of RBD-like and PH domains is crucial for yeast pheromone signaling.

The Ste5 protein forms a scaffold that associates and regulates the components of the mitogen-activated protein (MAP) kinase cascade that controls mating-pheromone-mediated signaling in the yeast Saccharomyces cerevisiae. Although it is known that the MEK kinase of the pathway, Ste11, associates with Ste5, details of this interaction have not been established. We identified a Ras-binding-domain-like (RBL) region in the Ste11 protein that is required specifically for the kinase to function in the mating pathway. This module is structurally related to domains in other proteins that mediate Ras-MAP kinase kinase kinase associations; however, this RBL module does not interact with Ras, but instead binds the PH domain of the Ste5 scaffold. Structural and functional studies suggest that the key role of this PH domain is to mediate the Ste5-Ste11 interaction. Overall these two evolutionarily conserved modules interact with each other through a unique interface, and thus in the pheromone pathway the structural context of the RBL domain contribution to kinase activation has been shifted through a change of its interaction partner from Ras to a PH domain.

Pubmed ID: 23242997 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | Amino Acid Substitution | Binding Sites | Genes, Mating Type, Fungal | MAP Kinase Kinase Kinases | Models, Molecular | Mutagenesis, Site-Directed | Peptide Mapping | Pheromones | Protein Binding | Protein Interaction Domains and Motifs | Protein Structure, Secondary | Protein Transport | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Signal Transduction

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Associated grants

  • Agency: Canadian Institutes of Health Research, Id: 42516-4
  • Agency: Canadian Institutes of Health Research, Id: GSP-48370

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A curated database that provides comprehensive integrated biological information for Saccharomyces cerevisiae along with search and analysis tools to explore these data. SGD allows researchers to discover functional relationships between sequence and gene products in fungi and higher organisms. The SGD also maintains the S. cerevisiae Gene Name Registry, a complete list of all gene names used in S. cerevisiae which includes a set of general guidelines to gene naming. Protein Page provides basic protein information calculated from the predicted sequence and contains links to a variety of secondary structure and tertiary structure resources. Yeast Biochemical Pathways allows users to view and search for biochemical reactions and pathways that occur in S. cerevisiae as well as map expression data onto the biochemical pathways. Literature citations are provided where available.


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SMART (a Simple Modular Architecture Research Tool) allows the identification and annotation of genetically mobile domains and the analysis of domain architectures. More than 500 domain families found in signaling, extracellular and chromatin-associated proteins are detectable. These domains are extensively annotated with respect to phyletic distributions, functional class, tertiary structures and functionally important residues. Each domain found in a non-redundant protein database as well as search parameters and taxonomic information are stored in a relational database system. User interfaces to this database allow searches for proteins containing specific combinations of domains in defined taxa. Users can use SMART in two different modes: normal or genomic. The main difference is in the underlying protein database used. In Normal SMART, the database contains Swiss-Prot, SP-TrEMBL and stable Ensembl proteomes. In Genomic SMART, only the proteomes of completely sequenced genomes are used; Ensembl for metazoans and Swiss-Prot for the rest. The protein database in Normal SMART has significant redundancy, even though identical proteins are removed. If a user uses SMART to explore domain architectures, or want to find exact domain counts in various genomes, consider switching to Genomic mode. The numbers in the domain annotation pages will be more accurate, and there will not be many protein fragments corresponding to the same gene in the architecture query results. Remember you are exploring a limited set of genomes, though. You can access SMART using our webservice. Check the WSDL file for details.


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BioInfoBank Meta Server

This service offers a gateway to well-benchmarked protein structure and function prediction methods. Structural models collected from the prediction servers are assessed using the powerful 3D-jury consensus approach. The Structure Prediction Meta Server provides access to various fold recognition, function prediction and local structure prediction methods. The Server takes the amino acid sequence of the query protein, the reference name for the prediction job, and the E-mail address as input. The E-mail address is used only for notification about errors during the execution of the job. The query sequence and the reference name are placed in the process queue. The Meta Server accepts only sequences, which have not been submitted before. In case of duplicate sequences the second user will be notified with a link to the previous submission. Sequences longer than 800 amino acids are not accepted by some services. The internal SQL database offers the possibility to find any previous jobs processed by the Meta Server using regular expressions addressing field like E-mail, Job Name and the host name, from which the job was initiated. Each server has its own process queuing system managed by the Meta Server. All results of fold recognition servers are translated into uniform formats. The information extracted from the raw output of the servers includes the PDB codes of the hits, the alignments and the similarity (reliability) scores specific for every server. Mapping of the hits to the SCOP and FSSP classifications are made either using known PDB representatives or alignment of the template sequence with the databases of proteins in both classifications. The secondary structure assignments for all hits are taken from the mapped FSSP (red for helices and blue for strands). Underscored amino acids indicate the first residue after an insertion in the template sequence. The Meta server provides translation of the alignments in standard formats like FASTA, PDB or CASP. The Meta Server is coupled to consensus servers. They provide jury predictions based on the results collected from other services. Not all fold recognition servers are used by the jury system. The data stored on the meta server is available through Jobs older than 2 months are not shown. The Meta Server is only a set of programs aimed to process and manage biological data, while the predictive power of the service comes from (mostly) remote prediction providers. Sponsors: This resource is supported by The BioInfoBank Institute.


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