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Background
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Histone acetylation, particularly of histone H4, has been proposed to play an important role in replication-dependent nucleosome assembly. The HAT1 protein contains D, A, and B motifs, which are present in many N-acetyltransferases, including those that acetylate substrates other than histones. The HAT1 holoenzyme consists of 2 subunits: the catalytic 46-kD HAT1 and the accessory p46. The p46 subunit stimulated the activity of HAT1 and bound to core histones. The HAT1 holoenzyme acetylated newly synthesized but not nucleosomal histone H4 at lys5 and lys12, and, to a lesser extent, histone H2A at lys5. HAT1 and p46 polypeptides are located in the nucleus of S-phase cells. HAT1 may play a role in telomeric silencing.
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Background
References
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- Gronroos, E., et al., Mol. Cell 10(3):483-493 (2002).
- Makowski, A.M., et al., J. Biol. Chem. 276(47):43499-43502 (2001).
- Cheung, P., et al., Mol. Cell 5(6):905-915 (2000).
- Verreault, A., et al., Curr. Biol. 8(2):96-108 (1998).
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