4.8 Article

Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

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NATURE CHEMICAL BIOLOGY
卷 8, 期 12, 页码 960-962

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NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.1093

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资金

  1. Biotechnology and Biological Sciences Research Council [BB/G014124/1]
  2. Wellcome Trust [091857/Z/10/Z]
  3. Cancer Research UK
  4. Slovenian Academy of Sciences and Arts
  5. Oxford Cancer Research Centre
  6. Oak Foundation
  7. BBSRC [BB/J003018/1, BB/D011523/1] Funding Source: UKRI
  8. Wellcome Trust [091857/Z/10/Z] Funding Source: Wellcome Trust
  9. Biotechnology and Biological Sciences Research Council [BB/D011523/1, BB/J003018/1, BB/G014124/1] Funding Source: researchfish

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The finding that oxygenase-catalyzed protein hydroxylation regulates animal transcription raises questions as to whether the translation machinery and prokaryotic proteins are analogously modified. Escherichia coli ycfD is a growth-regulating 2-oxoglutarate oxygenase catalyzing arginyl hydroxylation of the ribosomal protein Rpl16. Human ycfD homologs, Myc-induced nuclear antigen (MINA53) and NO66, are also linked to growth and catalyze histidyl hydroxylation of Rpl27a and Rpl8, respectively. This work reveals new therapeutic possibilities via oxygenase inhibition and by targeting modified over unmodified ribosomes.

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