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  Quantitative mass spectrometry and PAR-CLIP to identify RNA-protein interactions

Scheibe, M., Butter, F., Hafner, M., Tuschl, T., & Mann, M. (2012). Quantitative mass spectrometry and PAR-CLIP to identify RNA-protein interactions. NUCLEIC ACIDS RESEARCH, 40(19), 9897-9902. doi:10.1093/nar/gks746.

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This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/ by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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 Creators:
Scheibe, Marion1, Author           
Butter, Falk1, Author           
Hafner, Markus2, Author
Tuschl, Thomas3, Author           
Mann, Matthias1, Author           
Affiliations:
1Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
2external, ou_persistent22              
3Research Group of Combinatorical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578556              

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Free keywords: SITES; BRAIN
 Abstract: Systematic analysis of the RNA-protein interactome requires robust and scalable methods. We here show the combination of two completely orthogonal, generic techniques to identify RNA-protein interactions: PAR-CLIP reveals a collection of RNAs bound to a protein whereas SILAC-based RNA pull-downs identify a group of proteins bound to an RNA. We investigated binding sites for five different proteins (IGF2BP1-3, QKI and PUM2) exhibiting different binding patterns. We report near perfect agreement between the two approaches. Nevertheless, they are non-redundant, and ideally complement each other to map the RNA-protein interaction network.

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Language(s): eng - English
 Dates: 2012-08-092012-10
 Publication Status: Issued
 Pages: 6
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000310377200050
DOI: 10.1093/nar/gks746
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Title: NUCLEIC ACIDS RESEARCH
Source Genre: Journal
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Publ. Info: GREAT CLARENDON ST, OXFORD OX2 6DP, ENGLAND : OXFORD UNIV PRESS
Pages: - Volume / Issue: 40 (19) Sequence Number: - Start / End Page: 9897 - 9902 Identifier: ISSN: 0305-1048