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The human  ATRX  gene encodes hATRX, a chromatin-remodeling protein harboring an helicase/ATPase and ADD domains. The ADD domain has two zinc fingers that bind to histone tails and mediate hATRX binding to chromatin. dAtrx, the putative ATRX homolog in  Drosophila melanogaster , has a conserved helicase/ATPase domain but lacks the ADD domain. A bioinformatic search of the  Drosophila  genome using the human ADD sequence allowed us to identify the  CG8290  annotated gene, which encodes three ADD harboring- isoforms generated by alternative splicing. This  Drosophila  ADD domain is highly similar in structure and in the amino acids which mediate the histone tail contacts to the ADD domain of hATRX as shown by 3D modeling. Very recently the  CG8290  annotated gene has been named  dadd1 . We show through pull-down and CoIP assays that the products of the  dadd1  gene interact physically with dAtrx L  and HP1a and all of them mainly co-localize in the chromocenter, although euchromatic localization can also be observed through the chromosome arms. We confirm through ChIP analyses that these proteins are present  in vivo  in the same heterochromatic regions. The three isoforms are expressed throughout development. Flies carrying transheterozygous combinations of the  dadd1  and  atrx  alleles are semi-viable and have different phenotypes including the appearance of melanotic masses. Interestingly, the dAdd1-b and c isoforms have extra domains, such as MADF, which suggest newly acquired functions of these proteins. These results strongly support that, in  Drosophila , the  atrx  gene diverged and that the  dadd1 -encoded proteins participate with dAtrx in some cellular functions such as heterochromatin maintenance.

plos one

Characterization of the Drosophila Group Ortholog to the Amino-Terminus of the Alpha-Thalassemia and Mental Retardation X-Linked (ATRX) Vertebrate Protein