TY - JOUR
T1 - Human NAT10 is an ATP-dependent rna acetyltransferase responsible for N4-acetylcytidine formation in 18 S ribosomal RNA (rRNA)
AU - Suzuki, Tsutomu
AU - Ito, Satoshi
AU - Horikawa, Sayuri
AU - Suzuki, Tateki
AU - Kawauchi, Hiroki
AU - Tanaka, Yoshikazu
AU - Suzuki, Takeo
N1 - Publisher Copyright:
©© 2014 by The American Society for Biochemistry and Molecular Biology Inc.
PY - 2014/12/26
Y1 - 2014/12/26
N2 - 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 N4-acetylcytidine (ac4C) at position 1842 in the terminal helix of mammalian 18 S rRNA. RNAimediated 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 ac4C1842 formation catalyzed by NAT10 is involved in rRNA processing and ribosome biogenesis.
AB - 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 N4-acetylcytidine (ac4C) at position 1842 in the terminal helix of mammalian 18 S rRNA. RNAimediated 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 ac4C1842 formation catalyzed by NAT10 is involved in rRNA processing and ribosome biogenesis.
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U2 - 10.1074/jbc.C114.602698
DO - 10.1074/jbc.C114.602698
M3 - Article
C2 - 25411247
AN - SCOPUS:84919787527
SN - 0021-9258
VL - 289
SP - 35724
EP - 35730
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 52
ER -