Modifying the maker : oxygenases target ribosome biology

Research output: Contribution to journalArticlepeer-review

Authors

Colleges, School and Institutes

External organisations

  • Centre for Cellular and Molecular Physiology; University of Oxford; Oxford

Abstract

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.

Details

Original languageEnglish
Article numbere1009331
JournalTranslation
Volume3
Issue number1
Early online date3 Feb 2015
Publication statusPublished - 2015

Keywords

  • decoding, demethylase, hydroxylation, modification, oxygenase, ribosome, translation, 2-oxoglutarate