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

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

Authors

  • Nasertorabi F
  • Batisse C
  • Diepholz M
  • Suck D
  • Böttcher B

Journal

FEBS letters

Publication Data

July 21, 2011

Associated Grants

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

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