de Jong W W, Hendriks W
J Mol Evol. 1986;24(1-2):121-9. doi: 10.1007/BF02099960.
Comparative studies of the different families of lens-specific proteins of the vertebrates, the crystallins, and their genes reveal several interesting evolutionary features. The origin of alpha-crystallin can be traced back to the small heat shock proteins, while the superfamily of beta gamma-crystallins shows structural similarities with a bacterial spore coat protein. The crystallins display a great diversity within and between species, as well as during development. Ambiguous transcription, mRNA-processing, and translation contribute to this diversity of the crystallins and their expression. These mechanisms include the occurrence of atypical poly-A addition signals, alternative splicing, and the use of two initiation codons on a single mRNA.
对脊椎动物晶状体特异性蛋白质的不同家族(即晶状体蛋白)及其基因的比较研究揭示了几个有趣的进化特征。α-晶状体蛋白的起源可追溯到小热休克蛋白,而βγ-晶状体蛋白超家族与一种细菌芽孢衣蛋白具有结构相似性。晶状体蛋白在物种内部和物种之间以及发育过程中都表现出极大的多样性。模糊的转录、mRNA加工和翻译促成了晶状体蛋白及其表达的这种多样性。这些机制包括非典型多聚腺苷酸添加信号的出现、可变剪接以及在单个mRNA上使用两个起始密码子。