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The α-gliadin gene family. II. DNA and protein sequence variation, subfamily structure, and origins of pseudogenes

II. DNA and protein sequence variation, subfamily structure, and origins of pseudogenes

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Abstract

 The derived amino-acid sequences of all reported α-gliadin clones are compared and analyzed, and the patterns of sequence change within the α-gliadin family are examined. The most variable sequences are two polyglutamine domains. These two domains are characteristic features of the α-gliadin storage proteins and account for most of the variation in protein size of this otherwise highly conserved protein family. In addition, their encoding DNA sequences form microsatellites. Single-base substitutions in the α-gliadin genes show a preponderance of transitions, including the C to T substitution which contributes to the generation of stop codons, and consequently to the observation that approximately 50% of the α-gliadin genes are pseudogenes. In one unusual gene, a microsatellite has expanded to 321 bp as compared to the normal 36–72 bp, and may result from similar mechanisms that produce polyglutamine-associated genetic diseases in humans. A comparison of the 27 reported sequences show several α-gliadin gene subfamilies, at least some of which are genome specific.

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Received: 1 October 1996/Accepted: 20 December 1996

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Anderson, O., Greene, F. The α-gliadin gene family. II. DNA and protein sequence variation, subfamily structure, and origins of pseudogenes. Theor Appl Genet 95, 59–65 (1997). https://doi.org/10.1007/s001220050532

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  • DOI: https://doi.org/10.1007/s001220050532

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