Structural basis for the dimerization of Gemin5 and its role in protein recruitment and translation control.

ABSTRACT: In all organisms, a selected type of proteins accomplishes critical roles in cellular processes that govern gene expression. The multifunctional protein Gemin5 cooperates in translation control and ribosome binding, besides acting as the RNA-binding protein of the survival of motor neuron (SMN) complex. While these functions reside on distinct domains located at each end of the protein, the structure and function of the middle region remained unknown. Here, we solved the crystal structure of an extended tetratricopeptide (TPR)-like domain in human Gemin5 that self-assembles into a previously unknown canoe-shaped dimer. We further show that the dimerization module is functional in living cells driving the interaction between the viral-induced cleavage fragment p85 and the full-length Gemin5

SUBMITTER: Moreno-Morcillo M 

PROVIDER: S-EPMC6954437 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature