The alpha-gliadin gene family .2. DNA and protein sequence variation, subfamily structure, and origins of pseudogenes

The alpha-gliadin gene family .2. DNA and protein sequence variation, subfamily structure, and origins of pseudogenes
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DOI:
10.1007/s001220050532
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发表时间:
1997-07-01
影响因子:
5.4
通讯作者:
Greene, FC
Greene, FC
中科院分区:
农林科学1区
文献类型:
--
作者:
Anderson, OD;Greene, FC

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所有报道的α-麦醇溶蛋白克隆的衍生的氨基酸序列进行比较和分析,并检查α-麦醇溶蛋白家族内的序列变化的模式。最可变的序列是两个多聚谷氨酰胺结构域。这两个结构域是α-麦醇溶蛋白贮藏蛋白的特征性特征,并解释了该高度保守的蛋白质家族的蛋白质大小的大部分变化。此外,它们的编码DNA序列形成微卫星。α-麦醇溶蛋白基因中的单碱基取代显示出转换的优势,包括C至T的取代,其有助于终止密码子的产生,并因此观察到约50%的α-麦醇溶蛋白基因是假基因。在一个不寻常的基因中,一个微卫星与正常的36-72 bp相比已经扩展到321 bp,并且可能由产生人类多聚谷氨酰胺相关遗传疾病的类似机制引起。27个报道的序列的比较显示几个α-麦醇溶蛋白基因亚家族,其中至少有一些是基因组特异性的。
The derived amino-acid sequences of all reported alpha-gliadin clones are compared and analyzed, and the patterns of sequence change within the alpha-gliadin family are examined. The most variable sequences are two polyglutamine domains. These two domains are characteristic features of the alpha-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 alpha-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 alpha-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 alpha-gliadin gene subfamilies, at least some of which are genome specific.