Suppr超能文献

密西西比鳄和鬃狮蜥的α-晶体蛋白A序列:分子进化与爬行动物系统发育

alpha-Crystallin A sequences of Alligator mississippiensis and the lizard Tupinambis teguixin: molecular evolution and reptilian phylogeny.

作者信息

de Jong W W, Zweers A, Versteeg M, Dessauer H C, Goodman M

机构信息

Department of Biochemistry, University of Nijmegen, The Netherlands.

出版信息

Mol Biol Evol. 1985 Nov;2(6):484-93. doi: 10.1093/oxfordjournals.molbev.a040367.

Abstract

The amino acid sequences of the eye lens protein alpha-crystallin A from many mammalian and avian species, two frog species, and a dogfish have provided detailed information about the molecular evolution of this protein and allowed some useful inferences about phylogenetic relationships among these species. We now have isolated and sequenced the alpha-crystallins of the American alligator and the common tegu lizard. The reptilian alpha A chains appear to have evolved as slowly as those of other vertebrates, i.e., at two to three amino acid replacements per 100 residues in 100 Myr. The lack of charged replacements and the general types and distribution of replacements also are similar to those in other vertebrate alpha A chains. Maximum-parsimony analyses of the total data set of 67 vertebrate alpha A sequences support the monophyletic origin of alligator, tegu, and birds and favor the grouping of crocodilians and birds as surviving sister groups in the subclass Archosauria.

摘要

来自许多哺乳动物、鸟类、两种蛙类以及一种鲨鱼的眼晶状体蛋白α-晶状体蛋白A的氨基酸序列,提供了有关该蛋白质分子进化的详细信息,并使人们能够对这些物种之间的系统发育关系做出一些有用的推断。我们现在已经分离并测序了美国短吻鳄和普通鬃狮蜥的α-晶状体蛋白。爬行动物的αA链似乎与其他脊椎动物的进化速度一样缓慢,即在1亿年的时间里,每100个残基中有两到三个氨基酸替换。缺乏带电荷的替换以及替换的一般类型和分布也与其他脊椎动物的αA链相似。对67种脊椎动物αA序列的总数据集进行的最大简约分析支持短吻鳄、鬃狮蜥和鸟类的单系起源,并倾向于将鳄鱼和鸟类归为主龙次亚纲中现存的姐妹类群。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验