Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 289, Issue 52, Pages 35724-35730Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C114.602698
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Funding
- Ministry of Education, Science, Sports, and Culture of Japan
- Grants-in-Aid for Scientific Research [24000011, 26113003, 26560442, 26702035, 25620125, 26220205] Funding Source: KAKEN
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Human N-acetyltransferase 10 (NAT10) is known to be a lysine acetyltransferase that targets microtubules and histones and plays an important role in cell division. NAT10 is highly expressed in malignant tumors, and is also a promising target for therapies against laminopathies and premature aging. Here we report that NAT10 is an ATP-dependent RNA acetyltransferase responsible for formation of N-4-acetylcytidine (ac(4)C) at position 1842 in the terminal helix of mammalian 18 S rRNA. RNAi-mediated knockdown of NAT10 resulted in growth retardation of human cells, and this was accompanied by high-level accumulation of the 30 S precursor of 18 S rRNA, suggesting that ac(4)C1842 formation catalyzed by NAT10 is involved in rRNA processing and ribosome biogenesis.
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