Functional domains for assembly of histones H3 and H4 into the chromatin of Xenopus embryos

Lita Freeman, Hitoshi Kurumizaka, Alan P. Wolffe

研究成果: Article

37 引用 (Scopus)

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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 α-helix of the H4 histone fold domain are dispensable for chromatin assembly. The N-terminal tail and an N-terminal α-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.

元の言語English
ページ(範囲)12780-12785
ページ数6
ジャーナルProceedings of the National Academy of Sciences of the United States of America
93
発行部数23
DOI
出版物ステータスPublished - 1996 11 12
外部発表Yes

ASJC Scopus subject areas

  • Genetics
  • General

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