Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

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

doi

10.1021/bi602366n

subject

Has Abstract

pub_date

2007-02-27 00:00:00

pages

2091-9

issue

8

eissn

0006-2960

issn

1520-4995

journal_volume

46

pub_type

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