Modifying the maker : oxygenases target ribosome biology
Research output: Contribution to journal › Article › peer-review
Colleges, School and Institutes
- Centre for Cellular and Molecular Physiology; University of Oxford; Oxford
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.
|Early online date||3 Feb 2015|
|Publication status||Published - 2015|
- decoding, demethylase, hydroxylation, modification, oxygenase, ribosome, translation, 2-oxoglutarate