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-Structure paper
Title | Insights into the structure of the CCR4-NOT complex by electron microscopy. |
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Journal, issue, pages | FEBS Lett, Vol. 585, Issue 14, Page 2182-2186, Year 2011 |
Publish date | Jul 21, 2011 |
Authors | Fariborz Nasertorabi / Claire Batisse / Meikel Diepholz / Dietrich Suck / Bettina Böttcher / |
PubMed Abstract | 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 ...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. |
External links | FEBS Lett / PubMed:21669201 / PubMed Central |
Methods | EM (single particle) |
Resolution | 33.0 Å |
Structure data | EMDB-1901: |
Source |
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