Phosphorylation Drives a Dynamic Switch in Serine/Arginine-Rich Proteins
| Autor: | Volker Klaukien, Reinhard Lührmann, Markus Zweckstetter, ShengQi Xiang, Ralf Ficner, He-Hsuan Hsiao, Hai-Young Kim, Vytautas Gapsys, Henning Urlaub, Bert L. de Groot, Sergey Bessonov, Stefan Becker, Sina Möhlmann |
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| Rok vydání: | 2013 |
| Předmět: |
Magnetic Resonance Spectroscopy
Arginine metabolism [Arginine] chemistry [Arginine] chemistry [Nuclear Proteins] Biology Molecular Dynamics Simulation metabolism [RNA-Binding Proteins] Serine 03 medical and health sciences Molecular dynamics Splicing factor chemistry [RNA-Binding Proteins] Structural Biology chemistry [Serine] Phosphorylation Molecular Biology 030304 developmental biology RNA metabolism 0303 health sciences Serine-Arginine Splicing Factors metabolism [Serine] 030302 biochemistry & molecular biology Nuclear Proteins RNA-Binding Proteins Nuclear magnetic resonance spectroscopy Conformational entropy methods [Magnetic Resonance Spectroscopy] Biochemistry ddc:540 Biophysics metabolism [Nuclear Proteins] |
| Zdroj: | Structure Structure 21(12), 2162-2174 (2013). doi:10.1016/j.str.2013.09.014 |
| ISSN: | 0969-2126 |
| DOI: | 10.1016/j.str.2013.09.014 |
| Popis: | Summary 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 100 kDa SR-related protein hPrp28, for which phosphorylation at the RS repeat is required for spliceosome assembly. Thus, a phosphorylation-induced dynamic switch is common to the 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. |
| Databáze: | OpenAIRE |
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