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Architecture of the trypanosome RNA editing accessory complex, MRB1

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F12%3A00381882" target="_blank" >RIV/60077344:_____/12:00381882 - isvavai.cz</a>

  • Alternative codes found

    RIV/60076658:12310/12:43883517

  • Result on the web

    <a href="http://nar.oxfordjournals.org/content/40/12/5637.full" target="_blank" >http://nar.oxfordjournals.org/content/40/12/5637.full</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1093/nar/gks211" target="_blank" >10.1093/nar/gks211</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Architecture of the trypanosome RNA editing accessory complex, MRB1

  • Original language description

    Trypanosoma brucei undergoes an essential process of mitochondrial uridine insertion and deletion RNA editing catalyzed by a 20S editosome. The multiprotein mitochondrial RNA-binding complex 1 (MRB1) is emerging as an equally essential component of the trypanosome RNA editing machinery, with additional functions in gRNA and mRNA stabilization. The distinct and overlapping protein compositions of reported MRB1 complexes and diverse MRB1 functions suggest that the complex is composed of subcomplexes withRNA-dependent and independent interactions. To determine the architecture of the MRB1 complex, we performed a comprehensive yeast two-hybrid analysis of 31 reported MRB1 proteins. We also used in vivo analyses of tagged MRB1 components to confirm directand RNA-mediated interactions. Here, we show that MRB1 contains a core complex comprised of six proteins and maintained by numerous direct interactions. The MRB1 core associates with multiple subcomplexes and proteins through RNA-enhanced

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GA204%2F09%2F1667" target="_blank" >GA204/09/1667: Characterization of a novel protein complex involved in RNA processing and editing in the mitochondrion of Trypanosoma brucei</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2012

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Nucleic Acids Research

  • ISSN

    0305-1048

  • e-ISSN

  • Volume of the periodical

    40

  • Issue of the periodical within the volume

    12

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    14

  • Pages from-to

    5637-5650

  • UT code for WoS article

    000305829000046

  • EID of the result in the Scopus database