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TitleThe architecture of the Schizosaccharomyces pombe CCR4-NOT complex.
Journal, issue, pagesNat Commun, Vol. 7, Page 10433, Year 2016
Publish dateJan 25, 2016
AuthorsMarta Ukleja / Jorge Cuellar / Aleksandra Siwaszek / Joanna M Kasprzak / Mariusz Czarnocki-Cieciura / Janusz M Bujnicki / Andrzej Dziembowski / Jose M Valpuesta /
PubMed AbstractCCR4-NOT is a large protein complex present both in cytoplasm and the nucleus of eukaryotic cells. Although it is involved in a variety of distinct processes related to expression of genetic ...CCR4-NOT is a large protein complex present both in cytoplasm and the nucleus of eukaryotic cells. Although it is involved in a variety of distinct processes related to expression of genetic information such as poly(A) tail shortening, transcription regulation, nuclear export and protein degradation, there is only fragmentary information available on some of its nine subunits. Here we show a comprehensive structural characterization of the native CCR4-NOT complex from Schizosaccharomyces pombe. Our cryo-EM 3D reconstruction of the complex, combined with techniques such as immunomicroscopy, RNA-nanogold labelling, docking of the available high-resolution structures and models of different subunits and domains, allow us to propose its full molecular architecture. We locate all functionally defined domains endowed with deadenylating and ubiquitinating activities, the nucleus-specific RNA-interacting subunit Mmi1, as well as surfaces responsible for protein-protein interactions. This information provides insight into cooperation of the different CCR4-NOT complex functions.
External linksNat Commun / PubMed:26804377 / PubMed Central
MethodsEM (single particle)
Resolution20.0 Å
Structure data

EMDB-3232:
The architecture of the S. pombe CCR4-NOT complex
Method: EM (single particle) / Resolution: 20.0 Å

Source
  • Schizosaccharomyces pombe (fission yeast)

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