Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 36, Issue 1, Pages 7-18Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2010.07.002
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Funding
- Biotechnology and Biological Sciences Research Council
- The Wellcome Trust
- Cancer Research UK
- European Union
- Rhodes scholarship
- BBSRC [BB/D011523/1, BB/F006349/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/F006349/1, BB/D011523/1] Funding Source: researchfish
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Pioneering work in the 1960s defined prolyl and lysyl hydroxylations as physiologically important oxygenase-catalyzed modifications in collagen biosynthesis; subsequent studies demonstrated that extracellular epidermal growth factor-like domains were hydroxylated at aspartyl and asparaginyl residues. More recent work on the hypoxia-sensing mechanism in animals has shown that prolyl and asparaginyl hydroxylation of the hypoxia-inducible transcription factor play central roles in sensing hypoxia, by regulating protein protein interactions in an oxygen-dependent manner. The collective results imply that protein hydroxylation is more common than previously perceived. Most protein hydroxylases employ Fe(II) as a cofactor, and 2-oxoglutarate and oxygen as co-substrates. Related enzymes catalyze the demethylation of N-epsilon-methyl lysine residues in histones and of N-methylated nucleic acids, as well as hydroxylation of 5-methyl cytosine in DNA and 5-methoxycarbonylmethyluridine at the wobble position of tRNA. The combination of new molecular biological and analytical techniques is likely to reveal further roles for oxygenase-mediated modifications to biomacromolecules.
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