Histone acetyltransferase complexes: one size doesn't fit all.
Over the past 10 years, the study of histone acetyltransferases (HATs) has advanced significantly, and a number of HATs have been isolated from various organisms. It emerged that HATs are highly diverse and generally contain multiple subunits. The functions of the catalytic subunit depend largely on the context of the other subunits in the complex. We are just beginning to understand the specialized roles of HAT complexes in chromosome decondensation, DNA-damage repair and the modification of non-histone substrates, as well as their role in the broader epigenetic landscape, including the role of protein domains within HAT complexes and the dynamic interplay between HAT complexes and existing histone modifications.
Lee
Kenneth K
KK
Stowers Institute, 1000 East 50th Street, Kansas City, Missouri 64110, USA.
Workman
Jerry L
JL
D000818:Animals; D002843:Chromatin / Q000378:metabolism*; D004260:DNA Repair; D051548:Histone Acetyltransferases / Q000737:chemistry / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
D002843:Chromatin; D006657:Histones; D051548:Histone Acetyltransferases