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

Lita Freeman, Hitoshi Kurumizaka, Alan P. Wolffe

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)12780-12785
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume93
Issue number23
DOIs
Publication statusPublished - 1996 Nov 12
Externally publishedYes

ASJC Scopus subject areas

  • Genetics
  • General

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