Molecular Mechanism of SR Protein Kinase 1 Inhibition by the Herpes Virus Protein ICP27.

ABSTRACT: Serine-arginine (SR) protein kinase 1 (SRPK1) catalyzes the phosphorylation of SR proteins, which are a conserved family of splicing factors that contain a domain rich in arginine and serine repeats. SR proteins play important roles in constitutive pre-mRNA splicing and are also important regulators of alternative splicing. During herpes simplex virus infection, SRPK1 is inactivated and its cellular distribution is markedly altered by interaction with the viral protein ICP27, resulting in hypophosphorylation of SR proteins. Mutational analysis previously showed that the RGG box motif of ICP27 is required for interaction with SRPK1; however, the mechanism for the inhibition and the exact role of the RGG box was unknown. Here, we used solution nuclear magnetic resonance (NMR) spectroscopy an

SUBMITTER: Tunnicliffe RB 

PROVIDER: S-EPMC6805999 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature