Nardelli D, van het Schip F D, Gerber-Huber S, Haefliger J A, Gruber M, Ab G, Wahli W
Institut de Biologie Animale, Université de Lausanne, Switzerland.
J Biol Chem. 1987 Nov 15;262(32):15377-85.
The structural organization and the coding nucleotide sequence of the Xenopus laevis A2 and the chicken major vitellogenin genes have been compared. Both genes show the same exon-intron organization. However, the degree of homology between the nucleotide and derived amino acid sequences varies extensively along the genes. Several of the 35 exons are quite similar, and a unique cysteine motif in the lipovitellin II domain is conserved between the two genes. In contrast, one internal region is quite divergent. Part of this region encodes phosvitin, which appears to have evolved rapidly by both point mutations and duplications of serines or short other amino acid stretches. On the basis of these observations, we discuss the possible mechanism of evolution of phosvitin in vertebrates.
对非洲爪蟾的A2基因和鸡的主要卵黄生成素基因的结构组织及编码核苷酸序列进行了比较。这两个基因具有相同的外显子-内含子组织。然而，核苷酸序列和推导的氨基酸序列之间的同源程度在整个基因中差异很大。35个外显子中有几个非常相似，并且两个基因之间脂卵黄蛋白II结构域中一个独特的半胱氨酸基序是保守的。相比之下，一个内部区域差异很大。该区域的一部分编码卵黄高磷蛋白，它似乎通过点突变以及丝氨酸或其他短氨基酸片段的重复而快速进化。基于这些观察结果，我们讨论了脊椎动物中卵黄高磷蛋白可能的进化机制。
