Traut T W
Department of Biochemistry, University of North Carolina School of Medicine, Chapel Hill 27599-7260.
Proc Natl Acad Sci U S A. 1988 May;85(9):2944-8. doi: 10.1073/pnas.85.9.2944.
In considering the origin and evolution of proteins, the possibility that proteins evolved from exons coding for specific structure-function modules is attractive for its economy and simplicity but is not systematically supported by the available data. However, the number of correspondences between exons and units of protein structure-function that have so far been identified appears to be greater than expected by chance alone. The available data also show (i) that exons are fairly limited in size but are large enough to specify structure-function modules in proteins; (ii) that the position of introns for homologous domains in the same gene is reasonably stable, but there is also evidence for mechanisms that alter the position or existence of introns; and (iii) that it is possible that the observed relationship of exons to protein structure represents a degenerate state of an ancestral correspondence between exons and structure-function modules in proteins.
在考虑蛋白质的起源和进化时,蛋白质从编码特定结构 - 功能模块的外显子进化而来这一可能性因其经济性和简单性而颇具吸引力,但现有数据并未系统地支持这一观点。然而,迄今为止已确定的外显子与蛋白质结构 - 功能单元之间的对应数量似乎大于仅由偶然因素所预期的数量。现有数据还表明:(i)外显子的大小相当有限,但足以指定蛋白质中的结构 - 功能模块;(ii)同一基因中同源结构域的内含子位置相当稳定,但也有证据表明存在改变内含子位置或存在的机制;(iii)外显子与蛋白质结构之间观察到的关系可能代表了蛋白质中外显子与结构 - 功能模块之间祖先对应关系的一种退化状态。