PMC:1440874 / 2855-6777 JSONTXT

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Studies of X-chromosome inactivation in carrier females have demonstrated preferential inactivation of the chromosome bearing the abnormal allele in a variety of tissues [2], and this skewing of X-inactivation is thought to explain the mild phenotype observed in carriers.\nThe ATR-X syndrome is caused by mutations in a gene (ATRX) that comprises 36 exons spanning 300 kb of genomic DNA at Chromosome Xq13.3 [3]. This gene encodes two dominant protein isoforms (Figure 1). As well as the full-length ATRX protein of ~280 kDa, which is encoded by a transcript of ~10 kb, we recently demonstrated that a truncated isoform called ATRXt (~200 kDa) is produced from a transcript of around 7 kb, which arises when intron 11 fails to be spliced from the primary transcript and an alternative intronic poly(A) signal is used [4]. The mouse homolog of the ATRX gene, Atrx, is also situated on the X chromosome, and also gives rise to full-length (Atrx, ~280 kDa) and truncated (Atrxt, ~200 kDa) isoforms [4,5].\nFigure 1 Schematic Representation of the ATRX Isoforms\nShown at the top is the human ATRX cDNA. The boxes represent the 36 exons. The introns are not to scale. The alternative splicing of exons 6 and 7 is indicated. Shown underneath are the two ATRX protein isoforms. Full-length ATRX (~280 kDa) is encoded by the largest open reading frame. The positions of the principal features (the PHD-like domain and the seven SWI/SNF-like motifs) are indicated. Above full-length ATRX is shown the truncated ATRXt isoform (apparent molecular weight of ~200 kDa) that arises through the failure to splice intron 11 and the use of an intronic poly(A) signal. The intron-encoded region of ATRXt is indicated as a filled grey box. Locations of recombinant proteins (A2, FXNP5, and H-300) used to generate antibodies are shown. The scale bar represents 200 amino acids. Disease-causing missense mutations are clustered in two regions of the gene: a PHD-like zinc finger domain and a SNF2-like ATPase domain (Figure 1) [6]. The former motif is thought to be involved in protein-protein interactions in chromatin [7], and the latter is a feature of chromatin-remodelling proteins, and the presence of disease-causing mutations indicates the functional importance of these domains. ATRX has been shown to remodel chromatin [8]. It also interacts with HP1 at heterochromatin [9] and is recruited to promyelocytic leukemia nuclear bodies via an interaction with Daxx [10]. Furthermore, disruption of ATRX leads to diverse changes in DNA methylation [11]. Nevertheless, the role ATRX plays in gene expression remains unclear.\nThe consistent core of clinical and haematological features observed in ATR-X patients suggests that, like the SWI2/SNF2 chromatin-remodelling protein, ATRX probably regulates transcription of a discrete set of target genes. However, although there are clearly others to be found, at present the α-globin genes remain the only confirmed targets for transcriptional regulation by ATRX. Little is currently known about the precise role of the ATRX protein during mammalian development. To investigate the role of this protein during mouse development, we generated a conditionally deleted allele of the Atrx gene in mouse embryonic stem (ES) cells, and used these cells to examine the effect of ablating expression of the full-length Atrx protein in ES cells and in mouse 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