Functional domains for assembly of histones H3 and H4 into the chromatin of Xenopus embryos
AUTOR(ES)
Freeman, Lita
FONTE
The National Academy of Sciences of the USA
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=23997Documentos Relacionados
- The N-terminal domains of histones H3 and H4 are not necessary for chromatin assembly factor-1- mediated nucleosome assembly onto replicated DNA in vitro
- Heritable chromatin structure: Mapping “memory” in histones H3 and H4
- The highly conserved N-terminal domains of histones H3 and H4 are required for normal cell cycle progression.
- Histones H3 and H4 interact with the ends of nucleosome DNA.
- H3 and H4 histone cDNA sequences from Xenopus: a sequence comparison of H4 genes.