5′ Flanking Sequence and Structure of a Gene Encoding Rat 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase

The synthesis and degradation of fructose 2,6-bisphosphate, a ubiquitous stimulator of glycolysis, are catalyzed by 6-phosphofructo-2-kinase (EC 2.7.1.105) and fructose-2,6-bisphosphatase (EC 3.1.3.46), respectively. In liver, these two activities belong to separate domains of the same 470-residue p...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1989-09, Vol.86 (17), p.6543-6547
Main Authors: Darville, Martine I., Crepin, Karine M., Hue, Louis, Rousseau, Guy G.
Format: Article
Language:English
Subjects:
Animals
Base Sequence
Biological and medical sciences
Chromosome Mapping
Chromosomes
Cloning, Molecular
Complementary DNA
DNA
Enzymes
Exons
Fundamental and applied biological sciences. Psychology
Genes
Genes. Genome
Genomics
Introns
Liver
Liver - enzymology
Messenger RNA
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Nucleotides
Phosphofructokinase-2
Phosphoric Monoester Hydrolases - genetics
Phosphotransferases - genetics
Promoter Regions, Genetic
Rats
Restriction Mapping
RNA Splicing
RNA, Messenger - genetics
X Chromosome
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Summary:The synthesis and degradation of fructose 2,6-bisphosphate, a ubiquitous stimulator of glycolysis, are catalyzed by 6-phosphofructo-2-kinase (EC 2.7.1.105) and fructose-2,6-bisphosphatase (EC 3.1.3.46), respectively. In liver, these two activities belong to separate domains of the same 470-residue polypeptide. Various mRNAs have been described for this bifunctional enzyme, which is controlled by hormonal and metabolic signals. To understand the origin and regulation of these mRNAs, we have characterized rat genomic clones encoding the liver isozyme, which is regulated by cAMP-dependent protein kinase, and the muscle isozyme, which is not. We describe here a 55-kilobase gene that encodes these isozymes by alternative splicing from two promoters. Each of the putative promoters was sequenced over about 3 kilobases and found to include nucleotide motifs for binding regulatory factors. The two isozymes share the same 13 exons and differ only by the first exon that, in the liver but not in the muscle isozyme, contains the serine phosphorylated by cAMP-dependent protein kinase. The gene was assigned to the X chromosome. An analysis of the exon limits of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in relation to its functional domains and to its similarity with other proteins plus its G+C content at the third codon position suggests that this gene originates from several fusion events.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.86.17.6543