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  Investigation of protein–RNA interactions by mass spectrometry: Techniques and applications.

Schmidt, C., Kramer, K., & Urlaub, H. (2012). Investigation of protein–RNA interactions by mass spectrometry: Techniques and applications. Journal of proteomics, 75(12), 3478-3494. doi:10.1016/j.jprot.2012.04.030.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-C32D-1 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CE73-1
Genre: Journal Article

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1495647.pdf (Publisher version), 989KB
 
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Schmidt, C.1, Author              
Kramer, K.1, Author              
Urlaub, H.1, Author              
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1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Abstract: Protein–RNA complexes play many important roles in diverse cellular functions. They are involved in a wide variety of different processes in growth and differentiation at the various stages of the cell cycle. As their function and catalytic activity are directly coupled to the structural arrangement of their components—proteins and ribonucleic acids—the investigation of protein–RNA interactions is of great functional and structural importance. Here we discuss the most prominent examples of protein–RNA complexes and describe some frequently used purification strategies. We present various techniques and applications of mass spectrometry to study protein–RNA complexes. We discuss the analysis of intact complexes as well as proteomics-based and crosslinking-based approaches in which proteins are cleaved into smaller peptides. This article is part of a Special Section entitled: Understanding genome regulation and genetic diversity bymass spectrometry

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Language(s): eng - English
 Dates: 20122012
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.jprot.2012.04.030
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Title: Journal of proteomics
Source Genre: Journal
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Pages: - Volume / Issue: 75 (12) Sequence Number: - Start / End Page: 3478 - 3494 Identifier: -