Date of Award

1986

Document Type

Dissertation

Degree Name

Doctor of Philosophy (PhD)

Abstract

A rabbit genomic clone containing the muscle phosphofructokinase (PFK) gene of approximately 17 kilobase pairs encoding 779 amino acids was isolated and sequenced. This gene contains 22 exons, ranging from 45 to 190 base pairs, and is split by 21 introns of 73-3500 base pairs. Eighty six percent of this gene is occupied by introns. An additional incomplete intron is found in the 5' flanking region, while an Alu-like sequence is identified in the 3' flanking region. The amino acid sequence translated from the coding sequence of this gene reveals 29 residues (amino acid numbers 479-507) which complete a previously unidentified gap Poorman, R. A. et al., Nature, 309, 467 (1984) and 4 positions of discrepancy; Ser (--->) Arg (268), Leu (--->) Pro (442), Ile (--->) Ser (558), and the insertion of an additional Arg at position 565. Twelve exons encoding the N-half of the protein are scattered over 13 kbp and the other ten exons encoding the C-half are clustered in a length of 4 kbp. Most introns in this gene occupy positions between or at the ends of the secondary structural elements, but they are not located at identical positions in the two protein-coding halves of the gene. When these exons are identified with their encoded functional subdomains, the exon arrangement shows a duplication pattern between the two halves of the gene. These data support, at the gene level, the hypothesis that mammalian PFK evolved from a prokaryotic progenitor by gene duplication and divergence.

Pages

142

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