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Histones H3 and H4 have a well defined structural role in the nucleosome and an established role in the regulation of transcription. We have made use of a microinjection strategy using Xenopus embryos to define the minimal structural components of H3 and H4 necessary for nucleosome assembly into metazoan chromosomes in vivo. We find that both the N-terminal tail of H4, including all sites of acetylation, and the C-terminal alpha-helix of the H4 histone fold domain are dispensable for chromatin assembly. The N-terminal tail and an N-terminal alpha-helix of H3 are also dispensable for chromatin assembly. However, the remainder of the H3 and H4 histone folds are essential for incorporation of these proteins into chromatin. We suggest that elements of the histone fold domain maintain both nucleosomal integrity and have distinct functions essential for cell viability.
L Freeman, and
H Kurumizaka, and
A P Wolffe
July 2000,
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L Freeman, and
H Kurumizaka, and
A P Wolffe
November 1990,
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L Freeman, and
H Kurumizaka, and
A P Wolffe
December 2002,
Proceedings of the National Academy of Sciences of the United States of America,
L Freeman, and
H Kurumizaka, and
A P Wolffe
January 2005,
Annual review of cell and developmental biology,
L Freeman, and
H Kurumizaka, and
A P Wolffe
June 2017,
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L Freeman, and
H Kurumizaka, and
A P Wolffe
January 1997,
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L Freeman, and
H Kurumizaka, and
A P Wolffe
October 2005,
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L Freeman, and
H Kurumizaka, and
A P Wolffe
September 2002,
European journal of biochemistry,
L Freeman, and
H Kurumizaka, and
A P Wolffe
July 1982,
Cell,
L Freeman, and
H Kurumizaka, and
A P Wolffe
October 1996,
Cell,
