Molecular population genetics of an electrophoretically monomorphic protein in the alcohol dehydrogenase region of Drosophila pseudoobscura.
Molecular population genetics of an electrophoretically monomorphic protein in the alcohol dehydrogenase region of Drosophila pseudoobscura.
复制标题
假暗果蝇乙醇脱氢酶区域电泳单态蛋白的分子群体遗传学。
DOI：
10.1093/genetics/132.1.163
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发表时间：
1992
期刊：
影响因子：
3.3
通讯作者：
Miller,EL
中科院分区：
文献类型：
--
作者：
Schaeffer,SW;Miller,EL
使用 18 个假暗果蝇等染色体菌株的乙醇脱氢酶 (Adh) 区域的核苷酸序列数据来确定 ADH 中氨基酸多态性的缺乏是否是由于低中性突变率或最近的定向选择事件造成的。我们估计了 Adh 17 个亚区同义位点的中性突变参数 4Nmu。通过两个统计检验来测试核苷酸多样性数据是否偏离平衡中性模型。 Tajima 检验和 Hudson、Kreitman 和 Aguade 检验均未能拒绝中性模型。这些结果表明，假暗纹石斛的ADH酶缺乏氨基酸多态性，因为非同义位点的中性突变率较低。同义位点的中性突变参数在 Adh 区域的域之间是异质的。这些数据表明，对同义位点的选择性约束在功能域之间可能有所不同。
Nucleotide sequence data from the alcohol dehydrogenase (Adh) region of 18 isochromosomal strains of Drosophila pseudoobscura were used to determine whether the lack of amino acid polymorphism in ADH results from a low neutral mutation rate or a recent directional selection event. We estimated the neutral mutation parameter, 4Nmu, in synonymous sites for 17 subregions of Adh. The nucleotide diversity data were tested for departures from an equilibrium neutral model with two statistical tests. The Tajima test and the Hudson, Kreitman and Aguade test each failed to reject a neutral model. These results suggest that the ADH enzyme of D. pseudoobscura lacks amino acid polymorphisms because the neutral mutation rate of nonsynonymous sites is low. The neutral mutation parameter for synonymous sites is heterogeneous between domains of the Adh region. These data indicate that selective constrains on synonymous sites can vary between functional domains.