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Human Molecular Genetics, 1999, Vol. 8, No. 9 1807-1815
© 1999 Oxford University Press

A putative Drosophila homolog of the Huntington’s disease gene

Zhen Li+, Chris A. Karlovich+, Matthew P. Fish1, Matthew P. Scott1 and Richard M. Myers§

Department of Genetics and 1Departments of Developmental Biology and Genetics and Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, CA 94305-5120, USA

The Huntington’s disease (HD) gene encodes a protein, huntingtin, with no known function and no detectable sequence similarity to other proteins in current databases. To gain insight into the normal biological role of huntingtin, we isolated and sequenced a cDNA encoding a protein that is a likely homolog of the HD gene product in Drosophila melanogaster. We also determined the complete sequence of 43 125 contiguous base pairs of genomic DNA that encompass the Drosophila HD gene, allowing the intron–exon structure and 5"- and 3"-flanking regions to be delineated. The predicted Drosophila huntingtin protein has 3583 amino acids, which is several hundred amino acids larger than any other previously characterized member of the HD family. Analysis of the genomic and cDNA sequences indicates that Drosophila HD has 29 exons, compared with the 67 exons present in vertebrate HD genes, and that Drosophila huntingtin lacks the polyglutamine and polyproline stretches present in its mammalian counterparts. The Drosophila HD mRNA is expressed in a broad range of developmental stages and in the adult, a temporal pattern of expression similar to that observed for mammalian HD transcripts. We can discern five regions of high similarity from multiple sequence alignments between Drosophila and vertebrate huntingtins. These regions may define functionally important domains within the protein.

+ These authors contributed equally to this work

§ To whom correspondence should be addressed. Tel: +1 650 725 9687; Fax: +1 650 725 9689; Email: myers{at}shgc.stanford.edu


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