Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR.

ABSTRACT: Phosphorus-31 ((31)P) NMR can be used to characterize the structure and dynamics of phosphorylated proteins. Here, I use (31)P NMR to report on the chemical nature of a phosphothreonine that lies in the RNA binding domain of SLBP (stem-loop binding protein). SLBP is an intrinsically disordered protein and phosphorylation at this threonine promotes the assembly of the SLBP-RNA complex. The data show that the (31)P chemical shift can be a good spectroscopic probe for phosphate-coupled folding and binding processes in intrinsically disordered proteins, particularly where the phosphate exhibits torsional strain and is involved in a network of hydrogen-bonding interactions.

SUBMITTER: Thapar R 

PROVIDER: S-EPMC4215118 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature