Human histone acetyltransferase 1 protein preferentially acetylates H4 histone molecules in H3.1-H4 over H3.3-H4.

@article{Zhang2012HumanHA,
  title={Human histone acetyltransferase 1 protein preferentially acetylates H4 histone molecules in H3.1-H4 over H3.3-H4.},
  author={Hui Zhang and Junhong Han and Bin Kang and Rebecca Jodelle Burgess and Zhiguo Zhang},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 9},
  pages={
          6573-81
        }
}
In mammalian cells, canonical histone H3 (H3.1) and H3 variant (H3.3) differ by five amino acids and are assembled, along with histone H4, into nucleosomes via distinct nucleosome assembly pathways. H3.1-H4 molecules are assembled by histone chaperone CAF-1 in a replication-coupled process, whereas H3.3-H4 are assembled via HIRA in a replication-independent pathway. Newly synthesized histone H4 is acetylated at lysine 5 and 12 (H4K5,12) by histone acetyltransferase 1 (HAT1). However, it remains… CONTINUE READING
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