Structural Basis for the Rescue of Stalled Ribosomes: Structure of YaeJ Bound to the Ribosome

Author:

Gagnon Matthieu G.12,Seetharaman Sai V.12,Bulkley David3,Steitz Thomas A.132

Affiliation:

1. Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520–8114, USA.

2. Howard Hughes Medical Institute, Yale University, New Haven, CT 06520–8114, USA.

3. Department of Chemistry, Yale University, New Haven, CT 06520–8107, USA.

Abstract

Ribosome Rescue Ribosomes stall when they reach the end of defective messenger RNAs (mRNAs). In bacteria, the most-studied ribosomal rescue pathway involves a ribonucleoprotein complex comprising tmRNA (which acts as both transfer RNA and mRNA) and the protein SmpB. In an alternative pathway, some Gram-negative bacteria contain proteins that achieve tmRNA-independent rescue. Now, Neubauer et al. (p. 1366 ) present the structure of the Thermus thermophilus ribosome bound to a fragment of tmRNA, SmpB, and elongation factor Tu, and Gagnon et al. (p. 1370 ) report the structure of the T. thermophilus ribosome in complex with an initiator tRNA, a short mRNA fragment, and the rescue factor YaeJ. Though the two rescue systems are very different, both involve a protein tail that binds in the mRNA channel. This orients the rescue apparatus to facilitate switching translation to a different message in the tmRNA system or hydrolysis of peptidyl tRNA by YaeJ.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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