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Cloning and expression of novel isoforms of 6‐phosphofructo‐2‐kinase/fructose‐2,6‐bisphosphatase from bovine heart
Author(s) -
Vidal Hubert,
Crepin Karine M.,
Rider Mark H.,
Hue Louis,
Rousseau Guy G.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80898-5
Subject(s) - exon , gene isoform , isozyme , microbiology and biotechnology , cloning (programming) , messenger rna , phosphofructokinase 2 , gene , alternative splicing , biology , recombinant dna , phosphofructokinase , biochemistry , enzyme , glycolysis , computer science , programming language
Distinct 6‐phosphofructo‐2‐kinase (PFK‐2)/fructose 2,6‐bisphosphatase (FBPase‐2) cDNAs were cloned from bovine heart, showing that PFK‐2/FBPase‐2 gene B, which contains 16 exons, codes for at least five mRNAs. Three of them (B1, B2, B4) could encode the 58,000‐ M r isozyme. In B2 mRNA, exon 15 encodes four more residues than in Bl. In B4 mRNA, exon 15 encodes six more residues than in B1, butexon 16 (20 residues) is missing. B3 mRNA corresponds to the 54,000‐ M r isozyme. It lacks exon 15 and also differs from the other mRNAs in the 5' noncoding region. B5 mRNA encodes a truncated form. When expressed in E. coli , the recombinant isoforms corresponding to all these mRNAs except B5 exhibited PFK‐2 activity.