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A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F14%3A00079761" target="_blank" >RIV/00216224:14740/14:00079761 - isvavai.cz</a>

  • Result on the web

    <a href="http://www.jbc.org/content/289/41/28640.long" target="_blank" >http://www.jbc.org/content/289/41/28640.long</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1074/jbc.M114.592311" target="_blank" >10.1074/jbc.M114.592311</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    A Novel Protein-Protein Interaction in the RES (REtention and Splicing) Complex

  • Original language description

    The retention and splicing (RES) complex is a conserved spliceosome-associated module that was shown to enhance splicing of a subset of transcripts and promote the nuclear retention of unspliced pre-mRNAs in yeast. The heterotrimeric RES complex is organized around the Snu17p protein that binds to both the Bud13p and Pml1p subunits. Snu17p exhibits an RRM domain that resembles a U2AF homology motif (UHM) and Bud13p harbors a Trp residue reminiscent of an UHM-ligand motif (ULM). It has therefore been proposed that the interaction between Snu17p and Bud13p resembles canonical UHM-ULM complexes. Here, we have used biochemical and NMR structural analysis to characterize the structure of the yeast Snu17p-Bud13p complex. Unlike known UHMs that sequester theTrp residue of the ULM ligand in a hydrophobic pocket, Snu17p and Bud13p utilize a large interaction surface formed around the two helices of the Snu17p domain.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/EE2.3.20.0042" target="_blank" >EE2.3.20.0042: Internationalisation of the Structural Biology Research Programme with Emphasis on New Directions in R&D</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2014

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Journal of Biological Chemistry

  • ISSN

    0021-9258

  • e-ISSN

  • Volume of the periodical

    289

  • Issue of the periodical within the volume

    41

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    11

  • Pages from-to

    28640-28650

  • UT code for WoS article

    000343765400052

  • EID of the result in the Scopus database