Fiche publication
Date publication
mars 2017
Journal
Molecular and cellular biology
Auteurs
Membres identifiés du Cancéropôle Est :
Dr HAMICHE Ali
,
Dr RAMAIN Philippe
Tous les auteurs :
Fromental-Ramain C, Ramain P, Hamiche A
Lien Pubmed
Résumé
Histone variants are non-allelic isoforms of canonical histones and they are deposited, in contrast to canonical histones, in a replication-independent (RI) manner. RI deposition of H3.3, a histone variant from the H3.3 family, is mediated in mammals by distinct pathways involving either the histone regulator A (HIRA) complex or the death-associated protein (DAXX)/α-thalassemia X-linked mental retardation protein (ATRX) complex. Here, we investigated the function of Drosophila DAXX Like Protein (DLP) by using both fly genetics approaches and protein biochemistry. DLP specifically interacts with H3.3 and shows a prominent localization on the base of the X chromosome, where it appears to act in concert with XNP, the Drosophila homolog of ATRX, in heterochromatin assembly and maintenance. The functional association between DLP and XNP is further supported by a series of experiments, which illustrate genetic interactions and DLP-XNP-dependent localization of specific chromosomal proteins. In addition, DLP both participates in RI deposition of H3.3 and associates with the anti-silencing factor-1 (ASF1). We suggest, in agreement with a recently proposed model, that DLP and ASF1 are part of a pre-deposition complex, which is recruited by XNP and is necessary to prevent DNA exposure in the nucleus.
Mots clés
ASF1, DLP, H3.3, XNP, heterochromatin, histone variant
Référence
Mol. Cell. Biol.. 2017 Mar;:
