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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...

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Autores principales: Nasertorabi, Fariborz, Batisse, Claire, Diepholz, Meikel, Suck, Dietrich, Böttcher, Bettina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Science B.V 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3171648/
https://www.ncbi.nlm.nih.gov/pubmed/21669201
http://dx.doi.org/10.1016/j.febslet.2011.05.071
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author Nasertorabi, Fariborz
Batisse, Claire
Diepholz, Meikel
Suck, Dietrich
Böttcher, Bettina
author_facet Nasertorabi, Fariborz
Batisse, Claire
Diepholz, Meikel
Suck, Dietrich
Böttcher, Bettina
author_sort Nasertorabi, Fariborz
collection PubMed
description 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. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: CAF1 physically interacts with CCR4 and NOT1 by tandem affinity purification (View interaction)
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spelling pubmed-31716482011-09-30 Insights into the structure of the CCR4-NOT complex by electron microscopy Nasertorabi, Fariborz Batisse, Claire Diepholz, Meikel Suck, Dietrich Böttcher, Bettina FEBS Lett Article 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. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: CAF1 physically interacts with CCR4 and NOT1 by tandem affinity purification (View interaction) Elsevier Science B.V 2011-07-21 /pmc/articles/PMC3171648/ /pubmed/21669201 http://dx.doi.org/10.1016/j.febslet.2011.05.071 Text en © 2011 Elsevier B.V. https://creativecommons.org/licenses/by/3.0/ Open Access under CC BY 3.0 (https://creativecommons.org/licenses/by/3.0/) license
spellingShingle Article
Nasertorabi, Fariborz
Batisse, Claire
Diepholz, Meikel
Suck, Dietrich
Böttcher, Bettina
Insights into the structure of the CCR4-NOT complex by electron microscopy
title Insights into the structure of the CCR4-NOT complex by electron microscopy
title_full Insights into the structure of the CCR4-NOT complex by electron microscopy
title_fullStr Insights into the structure of the CCR4-NOT complex by electron microscopy
title_full_unstemmed Insights into the structure of the CCR4-NOT complex by electron microscopy
title_short Insights into the structure of the CCR4-NOT complex by electron microscopy
title_sort insights into the structure of the ccr4-not complex by electron microscopy
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3171648/
https://www.ncbi.nlm.nih.gov/pubmed/21669201
http://dx.doi.org/10.1016/j.febslet.2011.05.071
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