Benveniste-Schrode K, Doering J L, Hauck W W, Schrode J, Kendra K L, Drexler B K
J Mol Evol. 1985;22(3):209-19. doi: 10.1007/BF02099750.
Although the major types of vertebrate collagen have a number of structural properties in common, significant DNA sequence homologies have not been detected between different portions of the helical coding domains within the same gene or between different genes. However, under non-stringen hybridization conditions we found considerable cross-homology within and between alpha 1(I) and alpha 2(I) chick cDNAs in the coding regions for helical sequences. Detailed analyses at the DNA sequence level have led us to propose that the gene for chick pro alpha 2(I) collagen arose from a 9-bp primordial sequence. A consensus sequence for the 9-bp repeat was derived: GGTCCTCCT, which codes for a Gly-Pro-Pro triplet. The primordial ancestor of this 9-bp unit, GGTCCTXCT, apparently underwent duplication and divergence. Each resulting 9-bp sequence was triplicated to form a 27-bp domain, and a condensation event produced a 54-bp domain. This genetic unit then underwent multiple rounds of amplification to form the ancestral gene for the full-length helical section of alpha 2(I). A different 9-bp consensus sequence (GGTCCCCCC) seems to have been the basis of the chick pro alpha 1(I) gene.
虽然脊椎动物胶原蛋白的主要类型具有许多共同的结构特性,但在同一基因的螺旋编码域的不同部分之间或不同基因之间,尚未检测到显著的DNA序列同源性。然而,在非严格杂交条件下,我们发现在α1(I)和α2(I)鸡cDNA的螺旋序列编码区域内以及它们之间存在相当大的交叉同源性。在DNA序列水平上的详细分析使我们提出,鸡原α2(I)胶原蛋白基因起源于一个9碱基对的原始序列。推导出了这个9碱基对重复序列的共有序列:GGTCCTCCT,它编码一个甘氨酸-脯氨酸-脯氨酸三联体。这个9碱基对单元的原始祖先GGTCCTXCT显然经历了复制和分化。每个产生的9碱基对序列被三倍复制形成一个27碱基对的结构域,然后通过一次缩合事件产生一个54碱基对的结构域。这个遗传单元随后经历了多轮扩增,形成了α2(I)全长螺旋区的祖先基因。一个不同的9碱基对共有序列(GGTCCCCCC)似乎是鸡原α1(I)基因的基础。