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胶原蛋白基因的构建与进化。

Collagen gene construction and evolution.

作者信息

Runnegar B

出版信息

J Mol Evol. 1985;22(2):141-9. doi: 10.1007/BF02101692.

Abstract

Collagen genes appear to have been assembled by the tandem repetition of homologous primary (9 base pair), secondary (54 base pair), and tertiary (702 base pair) modules. In vertebrate interstitial collagen genes many of the secondary modules are separated by introns, but in invertebrate collagen genes the non-coding sequences lie near the ends of supposed tertiary modules and are therefore about 702 (54 X 13) base pairs apart. The genes for vertebrate interstitial collagens (types I-III) seem to have been constructed by the tandem repetition of five tertiary modules, three of which were subsequently shortened by internal deletions. This shortening of the gene resulted in the non-integral relationship between the period of the fibrils and the length of the molecules of vertebrate collagens, and was therefore responsible for the mechanical properties of the completed product. Comparisons of the amino acid sequences of various collagens indicate that the main types of collagen evolved about 800-900 million years ago, a date that agrees well with the fossil record of primitive Metazoa.

摘要

胶原蛋白基因似乎是由同源的一级(9个碱基对)、二级(54个碱基对)和三级(702个碱基对)模块串联重复组装而成。在脊椎动物的间质胶原蛋白基因中,许多二级模块被内含子隔开,但在无脊椎动物的胶原蛋白基因中,非编码序列位于假定的三级模块末端附近,因此相隔约702(54×13)个碱基对。脊椎动物间质胶原蛋白(I-III型)的基因似乎是由五个三级模块串联重复构建而成,其中三个随后因内部缺失而缩短。基因的这种缩短导致了脊椎动物胶原蛋白原纤维周期与分子长度之间的非整数关系,因此决定了最终产物的机械性能。对各种胶原蛋白氨基酸序列的比较表明,主要类型的胶原蛋白大约在8亿至9亿年前进化而来,这一日期与原始后生动物的化石记录非常吻合。

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