期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 290, 期 34, 页码 20712-20722出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R115.662627
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资金
- Wellcome Trust
- Cancer Research UK
- British Heart Foundation
- Biotechnology and Biological Sciences Research Council
- University of Oxford Clarendon Fund
- BBSRC [BB/L004275/1, BB/J003018/1, BB/L009846/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/J003018/1, BB/L009846/1, BB/L004275/1] Funding Source: researchfish
- Cancer Research UK [18245] Funding Source: researchfish
The post-translational hydroxylation of prolyl and lysyl residues, as catalyzed by 2-oxoglutarate (2OG)-dependent oxygenases, was first identified in collagen biosynthesis. 2OG oxygenases also catalyze prolyl and asparaginyl hydroxylation of the hypoxia-inducible factors that play important roles in the adaptive response to hypoxia. Subsequently, they have been shown to catalyze N-demethylation (via hydroxylation) of N-epsilon-methylated histone lysyl residues, as well as hydroxylation of multiple other residues. Recent work has identified roles for 2OG oxygenases in the modification of translation-associated proteins, which in some cases appears to be conserved from microorganisms through to humans. Here we give an overview of protein hydroxylation catalyzed by 2OG oxygenases, focusing on recent discoveries.
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