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Modifying the maker: Oxygenases target ribosome biology

The complexity of the eukaryotic protein synthesis machinery is partly driven by extensive and diverse modifications to associated proteins and RNAs. These modifications can have important roles in regulating translation factor activity and ribosome biogenesis and function. Further investigation of...

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Detalles Bibliográficos
Autores principales: Zhuang, Qinqin, Feng, Tianshu, Coleman, Mathew L
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4682802/
https://www.ncbi.nlm.nih.gov/pubmed/26779412
http://dx.doi.org/10.1080/21690731.2015.1009331
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author Zhuang, Qinqin
Feng, Tianshu
Coleman, Mathew L
author_facet Zhuang, Qinqin
Feng, Tianshu
Coleman, Mathew L
author_sort Zhuang, Qinqin
collection PubMed
description The complexity of the eukaryotic protein synthesis machinery is partly driven by extensive and diverse modifications to associated proteins and RNAs. These modifications can have important roles in regulating translation factor activity and ribosome biogenesis and function. Further investigation of ‘translational modifications’ is warranted considering the growing evidence implicating protein synthesis as a critical point of gene expression control that is commonly deregulated in disease. New evidence suggests that translation is a major new target for oxidative modifications, specifically hydroxylations and demethylations, which generally are catalyzed by a family of emerging oxygenase enzymes that act at the interface of nutrient availability and metabolism. This review summarizes what is currently known about the role or these enzymes in targeting rRNA synthesis, protein translation and associated cellular processes.
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spelling pubmed-46828022016-02-03 Modifying the maker: Oxygenases target ribosome biology Zhuang, Qinqin Feng, Tianshu Coleman, Mathew L Translation (Austin) Review The complexity of the eukaryotic protein synthesis machinery is partly driven by extensive and diverse modifications to associated proteins and RNAs. These modifications can have important roles in regulating translation factor activity and ribosome biogenesis and function. Further investigation of ‘translational modifications’ is warranted considering the growing evidence implicating protein synthesis as a critical point of gene expression control that is commonly deregulated in disease. New evidence suggests that translation is a major new target for oxidative modifications, specifically hydroxylations and demethylations, which generally are catalyzed by a family of emerging oxygenase enzymes that act at the interface of nutrient availability and metabolism. This review summarizes what is currently known about the role or these enzymes in targeting rRNA synthesis, protein translation and associated cellular processes. Taylor & Francis 2015-02-03 /pmc/articles/PMC4682802/ /pubmed/26779412 http://dx.doi.org/10.1080/21690731.2015.1009331 Text en © 2015 The Author(s). Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
spellingShingle Review
Zhuang, Qinqin
Feng, Tianshu
Coleman, Mathew L
Modifying the maker: Oxygenases target ribosome biology
title Modifying the maker: Oxygenases target ribosome biology
title_full Modifying the maker: Oxygenases target ribosome biology
title_fullStr Modifying the maker: Oxygenases target ribosome biology
title_full_unstemmed Modifying the maker: Oxygenases target ribosome biology
title_short Modifying the maker: Oxygenases target ribosome biology
title_sort modifying the maker: oxygenases target ribosome biology
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4682802/
https://www.ncbi.nlm.nih.gov/pubmed/26779412
http://dx.doi.org/10.1080/21690731.2015.1009331
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