ASF1 binds to a heterodimer of histones H3 and H4: a two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA. Academic Article uri icon

Overview

abstract

  • The first step in the formation of the nucleosome is commonly assumed to be the deposition of a histone H3-H4 heterotetramer onto DNA. Antisilencing function 1 (ASF1) is a major histone H3-H4 chaperone that deposits histones H3 and H4 onto DNA. With a goal of understanding the mechanism of deposition of histones H3 and H4 onto DNA, we have determined the stoichiometry of the Asf1-H3-H4 complex. We have established that a single molecule of Asf1 binds to an H3-H4 heterodimer using gel filtration, amino acid, reversed-phase chromatography, and analytical ultracentrifugation analyses. We demonstrate that Asf1 blocks formation of the H3-H4 heterotetramer by a mechanism that likely involves occlusion of the H3-H3 dimerization interface.

publication date

  • October 25, 2005

Research

keywords

  • Cell Cycle Proteins
  • DNA
  • Histones
  • Saccharomyces cerevisiae Proteins

Identity

PubMed Central ID

  • PMC4445473

Scopus Document Identifier

  • 27144453690

PubMed ID

  • 16229457

Additional Document Info

volume

  • 44

issue

  • 42