Lee C P, Kao M C, French B A, Putney S D, Chang S H
J Biol Chem. 1987 Mar 25;262(9):4195-9.
Sequence homologies between bacterial and rabbit muscle phosphofructokinases and between the amino- and carboxyl-terminal halves of the latter suggest that the mammalian enzyme evolved from a prokaryotic progenitor by gene duplication and divergence (Poorman, R. A., Randolph, A., Kemp, R. G., and Heinrikson, R. L. (1984) Nature 309, 467-469). We have isolated the gene for the rabbit enzyme and determined the nucleotide sequence for all the exons and most of the introns. This represents the first eukaryotic phosphofructokinase gene ever sequenced. The cloned gene is 17 kilobase pairs long. The coding sequence for 780 amino acids is split into 22 exons ranging in size from 15 to 63 codons. Sequence analysis shows that 75% of the bases at the third position of the codons in these exons are either G or C. Exons XV and XVI code for the 30 amino acid residues which were left unidentified in the published primary structure for this enzyme. When overlaid on the structure of the protein, most of the introns are located between or near the ends of the secondary structural elements but not at analogous positions in the two protein-coding halves of the gene.
细菌与兔肌肉磷酸果糖激酶之间以及兔肌肉磷酸果糖激酶氨基端与羧基端之间的序列同源性表明，哺乳动物的这种酶是通过基因复制和分化从原核生物祖先进化而来的（普尔曼，R. A.，伦道夫，A.，肯普，R. G.，以及海因里克森，R. L.（1984年）《自然》309卷，467 - 469页）。我们已经分离出兔磷酸果糖激酶的基因，并确定了所有外显子和大部分内含子的核苷酸序列。这是首次对真核生物磷酸果糖激酶基因进行测序。克隆的基因长度为17千碱基对。780个氨基酸的编码序列被分成22个外显子，大小从15到63个密码子不等。序列分析表明，这些外显子中密码子第三位的碱基75%是G或C。外显子XV和XVI编码该酶已发表一级结构中未确定的30个氨基酸残基。当与蛋白质结构重叠时，大多数内含子位于二级结构元件之间或其末端附近，但不在基因两个蛋白质编码部分的类似位置。
