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  Phosphorylation drives a dynamic switch in serine/arginine-rich proteins.

Xiang, S. Q., Gapsys, V., Kim, H. Y., Bessonov, S., Hsiao, H. H., Möhlmann, S., et al. (2013). Phosphorylation drives a dynamic switch in serine/arginine-rich proteins. Structure, 21(12), 2162-2174. doi:10.1016/j.str.2013.09.014.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-CE29-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CB4E-2
Genre: Journal Article

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 Creators:
Xiang, S. Q.1, Author              
Gapsys, V.2, Author              
Kim, H. Y., Author
Bessonov, S.3, Author              
Hsiao, H. H.4, Author              
Möhlmann, S., Author
Klaukien, V.5, Author              
Ficner, R., Author
Becker, S.5, Author              
Urlaub, H.4, Author              
Lührmann, R.3, Author              
de Groot, B.2, Author              
Zweckstetter, M.6, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society, ou_578571              
2Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              
3Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578576              
4Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              
5Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
6Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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 Abstract: Serine/arginine-rich (SR) proteins are important players in RNA metabolism and are extensively phosphorylated at serine residues in RS repeats. Here, we show that phosphorylation switches the RS domain of the serine/arginine-rich splicing factor 1 from a fully disordered state to a partially rigidified arch-like structure. Nuclear magnetic resonance spectroscopy in combination with molecular dynamics simulations revealed that the conformational switch is restricted to RS repeats, critically depends on the phosphate charge state and strongly decreases the conformational entropy of RS domains. The dynamic switch also occurs in the 100kDa SR-related protein hPrp28, for which phosphorylation at the RS repeat isrequired for spliceosome assembly. Thus, a phosphorylation-induced dynamic switch is common tothe class of serine/arginine-rich proteins and provides a molecular basis for the functional redundancy of serine/arginine-rich proteins and the profound influence of RS domain phosphorylation on protein-protein and protein-RNA interactions.

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Language(s): eng - English
 Dates: 2013-10-312013-12-03
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.str.2013.09.014
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Title: Structure
Source Genre: Journal
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Pages: - Volume / Issue: 21 (12) Sequence Number: - Start / End Page: 2162 - 2174 Identifier: -