Dbest1, a drosophila homolog of human bestrophin, is not required for viability or photoreceptor integrity

✍ Scribed by Beril C. Tavsanli; Kartik S. Pappu; Sunil Q. Mehta; Graeme Mardon

• Publisher: John Wiley and Sons
• Year: 2001
• Tongue: English
• Weight: 505 KB
• Volume: 31
• Category: Article
• ISSN: 1526-954X
• DOI: 10.1002/gene.10013

✦ Synopsis

Abstract

Summary: Best macular dystrophy (BMD) is an autosomal dominant human disease characterized by macular degeneration with juvenile onset (OMIM 153700). The disease is most often associated with mutations in Bestrophin, which encodes a novel protein with four putative transmembrane domains. However, complete loss‐of‐function mutations in Bestrophin have not been reported in humans or mice. We have identified three homologs of human Bestrophin in the Drosophila genome (dbest1‐3). The protein products of these three genes share significant homology to a 364 amino acid N‐terminal domain of human Bestrophin. We used P‐element mutagenesis to delete dbest1, which encodes a protein with the highest amino acid similarity to Bestrophin. Three independent dbest1 mutants were recovered from the mutagenesis screen. Homozygous null mutations in dbest1 do not significantly alter the viability or fertility of mutant flies. Moreover, dbest1 mutants have normal photoreceptor morphology and function. genesis 31:130–136, 2001. © 2001 Wiley‐Liss, Inc.