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首页> 外文期刊>Biochimica et Biophysica Acta. Protein Structure and Molecular Enzymology >Gene duplication and fusion have occurred frequently in the evolution of phosphagen kinases - a two-domain arginine kinase from the clam Pseudocardium sachalinensis
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Gene duplication and fusion have occurred frequently in the evolution of phosphagen kinases - a two-domain arginine kinase from the clam Pseudocardium sachalinensis

机译：基因复制和融合在磷酸酶激酶的进化中经常发生，磷酸酶激酶是蛤sa假心card的两个结构域的精氨酸激酶。

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摘要

In contrast to the 40 kDa arginine kinases from Molllusca and Arthropoda, the adductor muscle of the marine clam Pseudocardium sachalinensis contains an unusual arginine kinase consisting of an 86 kDa subunit. The cDNA encoding the 86 kDa arginine kinase was amplified by PCR and the cDNA-derived amino acid sequence of 724 residues was determined. The exact molecular mass for the protein was calculated to be 80 941 Da. The amino acid sequence clearly indicates that Pseudocardium arginine kinase has a two-domain structure: the first domain residues 1-363 and the second domain 364-724. The two domains, which are separated by an intron of 176 bp in the gene, show 62% amino acid sequence identity. This two-domain arginine kinase from a mollusc represents yet another multiple-domain enzyme observed in the phosphagen kinase enzyme family. Two-domain and three-domain enzymes have been observed in three other diverse invertebrate groups. Thus, it is clear that gene duplication and subsequent fusion have occurred frequently, and likely independently, during the course of the evolution of this enzyme family. Comparison of the amino acid sequence in the GS region (a possible candidate for the guanidine substrate recognition site in the phosphagen kinase family) suggests that the first domain of Pseudocardium arginine kinase might not retain a complete enzyme activity, because the Asp-7 in the GS region, which is assumed to be involved in the recognition of the positive charge of arginine, was replaced by a Gly residue in the first domain.
机译：与来自Molllusca和节肢动物的40 kDa精氨酸激酶相反，海洋蛤sa假单胞菌的内收肌包含一个由86 kDa亚基组成的不寻常的精氨酸激酶。通过PCR扩增编码86kDa精氨酸激酶的cDNA，并确定了来自724个残基的cDNA的氨基酸序列。该蛋白质的确切分子质量经计算为80 941 Da。氨基酸序列清楚地表明伪心氨酸精氨酸激酶具有两个结构域结构：第一结构域残基1-363和第二结构域364-724。由该基因中176 bp内含子分隔的两个域显示了62％的氨基酸序列同一性。来自软体动物的该两个结构域的精氨酸激酶代表了在磷酸酶激酶家族中观察到的另一种多结构域酶。在其他三个不同的无脊椎动物组中也观察到了两个域和三个域的酶。因此，很明显在该酶家族的进化过程中，基因重复和随后的融合经常发生，并且可能独立发生。 GS区（磷酸激酶家族中胍底物识别位点的可能候选者）中氨基酸序列的比较表明，伪心精氨酸激酶的第一个结构域可能无法保留完整的酶活性，因为在Asp-7中假定与精氨酸正电荷识别有关的GS区被第一结构域中的Gly残基取代。

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