Characterization of mammalian orthologues of the Drosophila osa gene: cDNA cloning, expression, chromosomal localization, and direct physical interaction with Brahma chromatin-remodeling complex

Genomics
Z KozmikC Vlcek

Abstract

The osa gene of Drosophila melanogaster encodes a nuclear protein that is a component of the Brahma chromatin-remodeling complex. Osa is required for embryonic segmentation, development of the notum and wing margin, and photoreceptor differentiation. In these tissues, osa mutations have effects opposite to those caused by wingless (wg) mutations, suggesting that osa functions as an antagonist of wg signaling. Here we describe the cloning and characterization of mammalian orthologues of osa. Three evolutionarily conserved domains were identified in Osa family members: the N-terminal Bright domain and C-terminally located Osa homology domains 1 and 2. RNase protection analysis indicates a widespread expression of the Osa1 gene during mouse development, in adult tissues, and in cultured cell lines. The Osa1 gene was localized to mouse chromosome 4, within the region syntenic to chromosomal position 1p35-p36 of its human counterpart. We present evidence that the OSA1 product is localized in the nucleus and associates with human Brahma complex, which suggests evolutionarily conserved function for Osa in gene regulation between mammals and Drosophila.

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Citations

Oct 15, 2010·The New England Journal of Medicine·Kimberly C WiegandDavid G Huntsman
Jan 11, 2005·Nucleic Acids Research·Antonia PatsialouElizabeth Moran
Sep 17, 2013·International Journal of Molecular Sciences·Eleftherios P SamartzisPatrick Imesch
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Oct 2, 2007·Progress in Retinal and Eye Research·Ales Cvekl, Melinda K Duncan
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Dec 2, 2010·The Biochemical Journal·Hiroko InoueNaoko Tanese
Feb 1, 2005·Developmental Biology·Elizabeth M CalleryGerald H Thomsen
Jun 1, 2005·Genomics·Deborah WilskerElizabeth Moran
Feb 24, 2009·Oncogene·D ReismanE A Thompson
Jun 8, 2011·Cell and Tissue Research·Angel Flores-AlcantarHilda Lomelí
Jun 2, 2004·The Biochemical Journal·Xiaomei WangElizabeth Moran

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