title: The MYST domain acetyltransferase Chameau functions in epigenetic mechanisms of transcriptional repression.
abstract: Reversible acetylation of histone tails plays an important role in chromatin remodelling and regulation of gene activity. While modification by histone acetyltransferase (HAT) is usually linked to transcriptional activation, we provide here evidence for HAT function in several types of epigenetic repression. Chameau (Chm), a new Drosophila member of the MYST HAT family, dominantly suppresses position effect variegation (PEV), is required for the maintenance of Hox gene silencing by Polycomb group (PcG) proteins, and can partially substitute for the MYST Sas2 HAT in yeast telomeric position effect (TPE). Finally, we provide in vivo evidence that the acetyltransferase activity of Chm is required in these processes, since a variant protein mutated in the catalytic domain no longer rescues PEV modification, telomeric silencing of SAS2-deficient yeast cells, nor lethality of chm mutant flies. These findings emphasize the role of an acetyltransferase in gene silencing, which supports, according to the histone code hypothesis, that transcription at a particular locus is determined by a precise combination of histone tail modifications rather than by overall acetylation levels.
authors: Laboratoire de Génétique et Physiologie du Développement, Institut de Biologie du Développement de Marseille, CNRS/INSERM/Université de la Méditerranée, Parc Scientifique de Luminy, Case 907, 13288 Marseille Cedex 9, France.
authors: Aurélie
authors: A
authors: Grienenberger
authors: Benoit
authors: B
authors: Miotto
authors: Thierry
authors: T
authors: Sagnier
authors: Giacomo
authors: G
authors: Cavalli
authors: Vera
authors: V
authors: Schramke
authors: Vincent
authors: V
authors: Geli
authors: Marie Christine
authors: MC
authors: Mariol
authors: Hélene
authors: H
authors: Berenger
authors: Yacine
authors: Y
authors: Graba
authors: Jacques
authors: J
authors: Pradel
mesh_terms: D000123:Acetyltransferases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism*; D000818:Animals; D004330:Drosophila / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D029721:Drosophila Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D018507:Gene Expression Regulation, Developmental; D020868:Gene Silencing; D006570:Heterochromatin / Q000502:physiology; D051548:Histone Acetyltransferases; D006657:Histones / Q000378:metabolism; D008297:Male; D009154:Mutation; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic; D014921:Wings, Animal / Q000502:physiology
chemical_list: D029721:Drosophila Proteins; D006570:Heterochromatin; D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases; C467710:chm protein, Drosophila; D051548:Histone Acetyltransferases