Format

Send to

Choose Destination
Structure. 2013 Dec 3;21(12):2162-74. doi: 10.1016/j.str.2013.09.014. Epub 2013 Oct 31.

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

Author information

1
Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry, Göttingen 37077, Germany.

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 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.

PMID:
24183573
DOI:
10.1016/j.str.2013.09.014
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center