Human proα1(I) collagen gene structure reveals evolutionary conservation of a pattern of introns and exons
Human proα1(I) collagen gene structure reveals evolutionary conservation of a pattern of introns and exons
复制标题
人类 proα1(I) 胶原蛋白基因结构揭示了内含子和外显子模式的进化保守性
作者：
M. Chu;W. Wet;M. Bernard;J. Ding;M. Morabito;J. Myers;C. Williams;F. Ramirez
胶原蛋白代表了一个有趣的例子，结构相关，但遗传上不同的蛋白质家族1。I型是脊椎动物胶原中含量最丰富的一种，包括两条proα1（I）链和一条proα2（I）链，每条链均含有末端前肽和338个（Gly，X，Y）重复的中心结构域。鸡proα2（I）基因的结构显示了外显子组织与（Gly，X，Y）重复序列排列之间有趣的关系（参见参考文献2的评论）。这导致了一个假设，即胶原蛋白是从一个54个碱基对（bp）的共同祖先单位进化而来的。在这里，我们展示了整个人proα1（I）基因的结构，并将其与鸡proα2（I）进行了比较。这两个基因的外显子排列非常相似，尽管人proα1（I）由于其内含子长度较短而更紧凑。这些数据有力地支持了这样一种观点，即I型基因是从祖先的多外显子单元进化而来的，一旦基因被翻译，强大的进化压力使其保持这种复杂的结构。
The collagens represent an interesting example of a structurally related but genetically distinct family of proteins1. Type I, the most abundant of the vertebrate collagens, comprises two proα1(I) chains and one proα2(I) chain, each containing terminal propeptides and a central domain of 338 (Gly, X, Y) repeats. The structure of the chicken proα2(I) gene shows an intriguing relationship between exon organization and the arrangement of (Gly, X, Y) repeats (see ref. 2 for review). This has led to the suggestion3 that the collagens evolved from a common ancestral unit of 54 base pairs (bp). Here we present the structure of the entire human proα1(I) gene and compare this with the chicken proα2(I). The exon arrangement of the two genes is remarkably similar, although the human proα1(I) is more compact because of the shorter length of its introns. The data strongly support the notion that the type I genes have evolved from an ancestral multi-exon unit, and that once the gene was translated, a strong evolutionary pressure caused it to maintain this elaborate structure.
编码鸡 II 型前胶原的基因组 DNA 的鉴定。
DOI：
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发表时间：
1983
期刊：
The Journal of biological chemistry
影响因子：
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作者：
Sandell,LJ;Yamada,Y;Dorfman,A;Upholt,WB
通讯作者：
Upholt,WB