Role of cytoplasmic acetyltransferases, NAA60 and HAT1, in cellular protection against genotoxic agents
Author:
Affiliation:
1. Laboratory of Biochemistry and Molecular Biology, Department of Medical Sciences, Faculty of Medicine, University of Miyazaki
2. Frontier Science Research Center, University of Miyazaki
Publisher
Japanese Society of Toxicology
Subject
General Medicine
Link
https://www.jstage.jst.go.jp/article/fts/9/6/9_179/_pdf
Reference20 articles.
1. Aksnes, H., Goris, M., Strømland, Ø., Drazic, A., Waheed, Q., Reuter, N. and Arnesen, T. (2017): Molecular determinants of the N-terminal acetyltransferase Naa60 anchoring to the Golgi membrane. J. Biol. Chem., 292, 6821-6837.
2. Aksnes, H., Van Damme, P., Goris, M., Starheim, K.K., Marie, M., et al. (2015): An organellar nα-acetyltransferase, naa60, acetylates cytosolic N termini of transmembrane proteins and maintains Golgi integrity. Cell Rep., 10, 1362-1374.
3. Barman, H.K., Takami, Y., Nishijima, H., Shibahara, K., Sanematsu, F. and Nakayama, T. (2008): Histone acetyltransferase-1 regulates integrity of cytosolic histone H3-H4 containing complex. Biochem. Biophys. Res. Commun., 373, 624-630.
4. Barman, H.K., Takami, Y., Ono, T., Nishijima, H., Sanematsu, F., Shibahara, K. and Nakayama, T. (2006): Histone acetyltransferase 1 is dispensable for replication-coupled chromatin assembly but contributes to recover DNA damages created following replication blockage in vertebrate cells. Biochem. Biophys. Res. Commun., 345, 1547-1557.
5. Deng, S. and Marmorstein, R. (2021): Protein N-Terminal Acetylation: Structural Basis, Mechanism, Versatility, and Regulation. Trends Biochem. Sci., 46, 15-27.
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