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Insights into the structure of the CCR4-NOT complex by electron microscopy.

FEBS letters | Jul 21, 2011

http://www.ncbi.nlm.nih.gov/pubmed/21669201

The CCR4-NOT complex is a deadenylation complex, which plays a major role for mRNA stability. The complex is conserved from yeast to human and consists of nine proteins NOT1-NOT5, CCR4, CAF1, CAF40 and CAF130. We have successfully isolated the complex using a Protein A tag on NOT1, followed by cross-linking on a glycerol gradient. All components of the complex were identified by mass spectrometry. Electron microscopy of negatively stained particles followed by image reconstruction revealed an L-shaped complex with two arms of similar length. The arms form an accessible cavity, which we think could provide an extensive interface for RNA-deadenylation.

Pubmed ID: 21669201 RIS Download

Mesh terms: Cell Cycle Proteins | Humans | Mass Spectrometry | Microscopy, Electron | Models, Molecular | Multiprotein Complexes | Protein Subunits | RNA, Messenger | Ribonucleases | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Transcription Factors

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Associated grants

  • Agency: Wellcome Trust, Id: 087658
  • Agency: NCRR NIH HHS, Id: P41 RR-0108
  • Agency: Wellcome Trust, Id: WT087658MA

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