Domain organization and intron positions in Caenorhabditis elegans collagen genes: the 54-bp module hypothesis revisited.
Domain organization and intron positions in Caenorhabditis elegans collagen genes: the 54-bp module hypothesis revisited.
复制标题
秀丽隐杆线虫胶原蛋白基因中的结构域组织和内含子位置：重新审视 54 bp 模块假设。
DOI：
10.1007/bf02143497
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发表时间：
1988
影响因子：
3.9
通讯作者：
Fields,C
中科院分区：
文献类型：
--
作者：
Fields,C
The amino acid (aa) sequences of the polypeptides encoded by five collagen genes of the nematodeCaenorhabditis elegans, col-6, col-7(partial),col-8, col-14, andcol-19, were determined. These collagen polypeptides, as well as those encoded by the previously sequencedC. eleganscollagen genescol-1andcol-2, share a common organization into five domains: an amino-terminal leader, a short (30–33 aa) (Gly-X-Y)ndomain, a non(Gly-X-Y) spacer, a long (127–132 aa) (Gly-X-Y)ndomain, and a short carboyl-terminal domain. The domain organizations and intron positions of these polypeptides were compared with those of the polypeptides encoded byDrosophilaandStrongylocentrotustype IV, and vertebrate types I, II, III, IV, and IX collagen genes; theC. eleganscollagen polypeptides are most similar to the vertebrate type IX collagents. It is suggested that the collagen gene family comprises two divergent subfamilies, one of which includes the vertebrate interstitial collagen genes, and the other of which includes the invertebrate collagen genes and the vertebrate type IV and type IX collagen genes. Only the vertebrate interstitial collagen genes display clear evidence of evolution via the tandem duplication of a 54-bp exon.
