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Interactions of the ribosome with mRNA and tRNA
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 st...
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Published in: | Current opinion in structural biology 2010-06, Vol.20 (3), p.325-332 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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. |
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ISSN: | 0959-440X 1879-033X |
DOI: | 10.1016/j.sbi.2010.03.002 |