Dorit R L, Ayala F J
Department of Biology, Yale University, New Haven, CT 06511, USA.
J Mol Evol. 1995 Jun;40(6):658-62. doi: 10.1007/BF00160514.
The evolution of any given protein reflects the interplay between proximal selective forces involving the conservation of protein structure and function and more general populational factors that shape the action and efficiency of natural selection. In an attempt to address that interplay, we have analyzed patterns of amino acid replacement within a well-conserved molecule, alcohol dehydrogenase (ADH), in the Drosophilidae. A sliding window, moved along the protein sequence in order to quantify the extent of change at each amino acid position, reveals heterogeneous amounts of replacement across the molecule when all ADH sequences are analyzed simultaneously. Surprisingly, the replacement profile for ADH differs significantly in the melanogaster, mulleri, and Hawaiian subgroups, reflecting the imprint of the differing evolutionary histories of each of these assemblages on the evolution of this conservative molecule.
任何特定蛋白质的进化反映了近端选择力（涉及蛋白质结构和功能的保守性）与更一般的群体因素（塑造自然选择的作用和效率）之间的相互作用。为了研究这种相互作用，我们分析了果蝇科中一个保守性良好的分子——乙醇脱氢酶（ADH）内的氨基酸替换模式。一个沿着蛋白质序列移动的滑动窗口，用于量化每个氨基酸位置的变化程度，当同时分析所有ADH序列时，揭示了整个分子中不同程度的替换。令人惊讶的是，ADH的替换图谱在黑腹果蝇亚组、穆勒果蝇亚组和夏威夷果蝇亚组中存在显著差异，这反映了这些分类群各自不同的进化历史对这个保守分子进化的影响。
