| Literature DB >> 20392630 |
Natalia Demeshkina1, Lasse Jenner, Gulnara Yusupova, Marat Yusupov.
Abstract
Recent collection of high-resolution crystal structures of the 70S ribosome with mRNA and tRNA substrates enhances our knowledge of protein synthesis principles. A novel network of interactions between the ribosome in the elongation state and mRNA downstream from the A codon suggests that mRNA is stabilized and aligned at the entrance to the decoding center. The X-ray studies clarify how natural modifications of tRNA are involved in the stabilization of the codon-anticodon interactions, prevention of frame-shifting and also expansion of the decoding capacity of tRNAs. In addition, the crystal structures provide the view that tRNA in the A and P sites communicate through a protein rich environment and suggest how these tRNAs are controlled through the intersubunit bridge formed by protein L31. Crown Copyright 2010. Published by Elsevier Ltd. All rights reserved.Entities:
Mesh:
Substances:
Year: 2010 PMID: 20392630 DOI: 10.1016/j.sbi.2010.03.002
Source DB: PubMed Journal: Curr Opin Struct Biol ISSN: 0959-440X Impact factor: 6.809