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

MPG-Autoren
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Xiang,  S. Q.
Research Group of Protein Structure Determination using NMR, MPI for Biophysical Chemistry, Max Planck Society;

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Gapsys,  V.
Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Bessonov,  S.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Hsiao,  H. H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Klaukien,  V.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

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Lührmann,  R.
Department of Cellular Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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de Groot,  B.
Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Zweckstetter,  M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

Volltexte (frei zugänglich)

1877941.pdf
(Verlagsversion), 4MB

Ergänzendes Material (frei zugänglich)

1877941_Suppl_1.pdf
(Ergänzendes Material), 2MB

Zitation

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.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0014-CE29-E
Zusammenfassung
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.