Skip to Content
Merck
  • Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis.

Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis.

Cell (2004-01-14)
Hideaki Tagami, Dominique Ray-Gallet, Geneviève Almouzni, Yoshihiro Nakatani
ABSTRACT

Deposition of the major histone H3 (H3.1) is coupled to DNA synthesis during DNA replication and possibly DNA repair, whereas histone variant H3.3 serves as the replacement variant for the DNA-synthesis-independent deposition pathway. To address how histones H3.1 and H3.3 are deposited into chromatin through distinct pathways, we have purified deposition machineries for these histones. The H3.1 and H3.3 complexes contain distinct histone chaperones, CAF-1 and HIRA, that we show are necessary to mediate DNA-synthesis-dependent and -independent nucleosome assembly, respectively. Notably, these complexes possess one molecule each of H3.1/H3.3 and H4, suggesting that histones H3 and H4 exist as dimeric units that are important intermediates in nucleosome formation. This finding provides new insights into possible mechanisms for maintenance of epigenetic information after chromatin duplication.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Histone H3 peptide (1-21) human, ≥90% (HPLC)
Pricing and availability is not currently available.
Sigma-Aldrich
LSD1 substrate (Di-methylated K4_H3), ≥90% (HPLC)
Pricing and availability is not currently available.
Sigma-Aldrich
Histone H3.1 human
Pricing and availability is not currently available.