Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-35601
Biochemistry 2007 Feb 27;468:2091-9. doi: 10.1021/bi602366n.
Show Gene links Show Anatomy links

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

Berndsen CE , Selleck W , McBryant SJ , Hansen JC , Tan S , Denu JM .


Abstract
The mechanisms by which multisubunit histone acetyltransferase (HAT) complexes recognize and perform efficient acetylation on nucleosome substrates are largely unknown. Here, we use a variety of biochemical approaches and compare histone-based substrates of increasing complexity to determine the critical components of nucleosome recognition by the MOZ, Ybf2/Sas3, Sas2, Tip60 family HAT complex, Piccolo NuA4 (picNuA4). We find the histone tails to be dispensable for binding to both nucleosomes and free histones and that the H2A, H3, and H2B tails do not influence the ability of picNuA4 to tetra-acetylate the H4 tail within the nucleosome. Most notably, we discovered that the histone-fold domain (HFD) regions of histones, particularly residues 21-52 of H4, are critical for tight binding and efficient tail acetylation. Presented evidence suggests that picNuA4 recognizes the open surface of the nucleosome on which the HFD of H4 is located. This binding mechanism serves to direct substrate access to the tails of H4 and H2A and allows the enzyme to be "tethered", thereby increasing the effective concentration of the histone tail and permitting successive cycles of H4 tail acetylation.

PubMed ID: 17274630
PMC ID: PMC1994252
Article link: Biochemistry
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: h2ac21 h2bc21 kat5 kat6a pclo

References [+] :
ALLFREY, ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS. 1964, Pubmed