Ribosomes in the balance: structural equilibrium ensures translational fidelity and proper gene expression.

ABSTRACT: At equilibrium, empty ribosomes freely transit between the rotated and un-rotated states. In the cell, the binding of two translation elongation factors to the same general region of the ribosome stabilizes one state over the other. These stabilized states are resolved by expenditure of energy in the form of GTP hydrolysis. A prior study employing mutants of a late assembling peripheral ribosomal protein suggested that ribosome rotational status determines its affinity for elongation factors, and hence translational fidelity and gene expression. Here, mutants of the early assembling integral ribosomal protein uL2 are used to test the generality of this hypothesis. rRNA structure probing analyses reveal that mutations in the uL2 B7b bridge region shift the equilibrium toward the rotated sta

SUBMITTER: Musalgaonkar S 

PROVIDER: S-EPMC4245932 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature