Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 41, Issue 9, Pages 798-814Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2016.06.001
Keywords
-
Categories
Funding
- French National Research Agency [ANR-15-CE11-0021-01]
- LABEX [ANR-10-LABX-0036_NETRNA]
- European Research Council [294312]
- Agence Nationale de la Recherche (ANR) [ANR-15-CE11-0021] Funding Source: Agence Nationale de la Recherche (ANR)
Ask authors/readers for more resources
The fidelity of translation depends strongly on the selection of the correct aminoacyl-tRNA that is complementary to the mRNA codon present in the ribosomal decoding center. The ribosome occasionally makes mistakes by selecting the wrong substrate from the pool of aminoacyl-tRNAs. Here, we summarize recent structural advances that may help to clarify the origin of missense errors that occur during decoding. These developments suggest that discrimination between tRNAs is based primarily on steric complementarity and shape acceptance rather than on the number of hydrogen bonds between the molding of the decoding center and the codon-anticodon duplex. They strengthen the hypothesis that spatial mimicry, due either to base tautomerism or ionization, drives infidelity in ribosomal translation.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available