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Mistranslation and its control by tRNA synthetases
Aminoacyl tRNA synthetases are ancient proteins that interpret the genetic material in all life forms. They are thought to have appeared during the transition from the RNA world to the theatre of proteins. During translation, they establish the rules of the genetic code, whereby each amino acid is a...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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The Royal Society
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3158927/ https://www.ncbi.nlm.nih.gov/pubmed/21930589 http://dx.doi.org/10.1098/rstb.2011.0158 |
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author | Schimmel, Paul |
author_facet | Schimmel, Paul |
author_sort | Schimmel, Paul |
collection | PubMed |
description | Aminoacyl tRNA synthetases are ancient proteins that interpret the genetic material in all life forms. They are thought to have appeared during the transition from the RNA world to the theatre of proteins. During translation, they establish the rules of the genetic code, whereby each amino acid is attached to a tRNA that is cognate to the amino acid. Mistranslation occurs when an amino acid is attached to the wrong tRNA and subsequently is misplaced in a nascent protein. Mistranslation can be toxic to bacteria and mammalian cells, and can lead to heritable mutations. The great challenge for nature appears to be serine-for-alanine mistranslation, where even small amounts of this mistranslation cause severe neuropathologies in the mouse. To minimize serine-for-alanine mistranslation, powerful selective pressures developed to prevent mistranslation through a special editing activity imbedded within alanyl-tRNA synthetases (AlaRSs). However, serine-for-alanine mistranslation is so challenging that a separate, genome-encoded fragment of the editing domain of AlaRS is distributed throughout the Tree of Life to redundantly prevent serine-to-alanine mistranslation. Detailed X-ray structural and functional analysis shed light on why serine-for-alanine mistranslation is a universal problem, and on the selective pressures that engendered the appearance of AlaXps at the base of the Tree of Life. |
format | Online Article Text |
id | pubmed-3158927 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The Royal Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-31589272011-10-27 Mistranslation and its control by tRNA synthetases Schimmel, Paul Philos Trans R Soc Lond B Biol Sci Articles Aminoacyl tRNA synthetases are ancient proteins that interpret the genetic material in all life forms. They are thought to have appeared during the transition from the RNA world to the theatre of proteins. During translation, they establish the rules of the genetic code, whereby each amino acid is attached to a tRNA that is cognate to the amino acid. Mistranslation occurs when an amino acid is attached to the wrong tRNA and subsequently is misplaced in a nascent protein. Mistranslation can be toxic to bacteria and mammalian cells, and can lead to heritable mutations. The great challenge for nature appears to be serine-for-alanine mistranslation, where even small amounts of this mistranslation cause severe neuropathologies in the mouse. To minimize serine-for-alanine mistranslation, powerful selective pressures developed to prevent mistranslation through a special editing activity imbedded within alanyl-tRNA synthetases (AlaRSs). However, serine-for-alanine mistranslation is so challenging that a separate, genome-encoded fragment of the editing domain of AlaRS is distributed throughout the Tree of Life to redundantly prevent serine-to-alanine mistranslation. Detailed X-ray structural and functional analysis shed light on why serine-for-alanine mistranslation is a universal problem, and on the selective pressures that engendered the appearance of AlaXps at the base of the Tree of Life. The Royal Society 2011-10-27 /pmc/articles/PMC3158927/ /pubmed/21930589 http://dx.doi.org/10.1098/rstb.2011.0158 Text en This journal is © 2011 The Royal Society http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Articles Schimmel, Paul Mistranslation and its control by tRNA synthetases |
title | Mistranslation and its control by tRNA synthetases |
title_full | Mistranslation and its control by tRNA synthetases |
title_fullStr | Mistranslation and its control by tRNA synthetases |
title_full_unstemmed | Mistranslation and its control by tRNA synthetases |
title_short | Mistranslation and its control by tRNA synthetases |
title_sort | mistranslation and its control by trna synthetases |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3158927/ https://www.ncbi.nlm.nih.gov/pubmed/21930589 http://dx.doi.org/10.1098/rstb.2011.0158 |
work_keys_str_mv | AT schimmelpaul mistranslationanditscontrolbytrnasynthetases |