Structural plasticity of histones H3-H4 facilitates their allosteric exchange between RbAp48 and ASF1

Wei Zhang, Marek Tyl, Richard Ward, Frank Sobott, Joseph Maman, Andal S. Murthy, Aleksandra A. Watson, Oleg Fedorov, Andrew Bowman, Tom Owen-Hughes, Hassane El Mkami, Natalia V. Murzina, David G. Norman, Ernest D. Laue*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

45 Citations (Scopus)

Abstract

The mechanisms by which histones are disassembled and reassembled into nucleosomes and chromatin structure during DNA replication, repair and transcription are poorly understood. A better understanding of the processes involved is, however, crucial if we are to understand whether and how histone variants and post-translationally modified histones are inherited in an epigenetic manner. To this end we have studied the interaction of the histone H3-H4 complex with the human retinoblastoma-associated protein RbAp48 and their exchange with a second histone chaperone, anti-silencing function protein 1 (ASF1). Exchange of histones H3-H4 between these two histone chaperones has a central role in the assembly of new nucleosomes, and we show here that the H3-H4 complex has an unexpected structural plasticity, which is important for this exchange.

Original languageEnglish
Pages (from-to)29-35
Number of pages7
JournalNature Structural and Molecular Biology
Volume20
Issue number1
DOIs
Publication statusPublished - Jan 2013

Keywords

  • DNA-REPLICATION
  • PULSED EPR
  • CHROMATIN
  • NUCLEOSOME
  • H4
  • COMPLEX
  • H3
  • METHYLATION
  • SUBUNIT
  • YEAST

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