Complete nucleotide sequence coding for rat liver 6‐phosphofructo‐2‐kinase/fructose‐2,6‐bisphosphatase derived from a cDNA clone

Darville, Martine I.; Crepin, Karine M.; Vandekerckhove, Joël; Damme, Jozef Van; Octave, Jean‐Noël; Rider, Mark H.; Marchand, Maurice; Hue, Louis; Rousseau, Guy

doi:10.1016/0014-5793(87)80476-3

Cited by 78 publications

(53 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The best characterized are the liver (L), skeletal muscle (M), heart (H), testis (T) and brain isoenzymes. The sequence of the L mRNA of several species is known [30][31][32] as well as that of the rat M-, T-and H-type mRNAs [33][34][35][36]. In addition, a fetal (F)-type mRNA was recently identified [37].…”

Section: Gene Organizationmentioning

confidence: 99%

Transcriptional control of genes that regulate glycolysis and gluconeogenesis in adult liver

Lemaigre¹,

Rousseau²

1994

Biochemical Journal

100

View full text Add to dashboard Cite

Section: Gene Organizationmentioning

confidence: 99%

Transcriptional control of genes that regulate glycolysis and gluconeogenesis in adult liver

Lemaigre¹,

Rousseau²

1994

Biochemical Journal

100

View full text Add to dashboard Cite

“…This bifunctional enzyme also exhibits intriguing similarities with phosphoglycerate mutase [PGAM; EC 5. 4 13 of which are common to the two isozymes. Part of this work has been presented in the form of an abstract (9).…”

mentioning

confidence: 99%

5' flanking sequence and structure of a gene encoding rat 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.

Darville¹,

Crepin²,

Hue³

et al. 1989

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

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 cAMPdependent protein kinase. The gene was assigned to the X chromosome. An analysis ofthe exon limits of6-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.Fructose 2,6-bisphosphate is the most potent allosteric stimulator of 6-phosphofructo-1-kinase (EC 2.7.1.11), a key enzyme of glycolysis. The synthesis of fructose 2,6-bisphosphate is catalyzed by 6-phosphofructo-2-kinase (PFK-2; EC 2.7.1.105) and its degradation is catalyzed by fructose-2,6-bisphosphatase (FBPase-2; EC 3.1.3.46). In liver, these two activities belong to separate domains of each subunit (470 amino acids) of the same homodimeric protein. This bifunctional enzyme integrates a number of hormonal and metabolic signals including cAMP. In fibroblasts, PFK-2 activity is stimulated by growth factors, tumor promoters, and tyrosinespecific oncogenic protein kinases (1, 2).Biochemical and immunologic data suggest the existence of distinct PFK-2/FBPase-2 isozymes. Using PFK-2/ FBPase-2 cDNA probes from rat liver (4), we have identified a 2.1-kilobase (kb) mRNA coding for the liver (L) isozyme, a 1.9-kb mRNA coding for the skeletal muscle (M) isozyme, and a 6.8-kb mRNA presumably coding for the heart isozyme (5). The L and M isozymes have a common sequence of438 amino acids and differ only at the N terminus. In the L isozyme, the divergent sequence is 32 residues long and includes the serine (Ser-32) phosphorylated by cAMP-dependent protein kinase. In the M isozyme, the N terminus is 10 residues long and is unrelated to the unique part of the L isozyme. Expression of the L, but not the M, isozyme of PFK-2/FBPase-2 is controlled by diet and insulin (6, 7). This gene is 55 kb long and contains 15 exons, 13 of which are common to the two isozymes. Part of this work has been presented in the form of an abstract (9). MATERIALS...

show abstract

“…Comparison of protein sequence of mouse 2kbC5 to rat PFK-2/FBPase-2 isozymes. Alignment is shown for PFK-2/FBPase-2 isozymes: partial rat heart-type sequence [6]; mouse 2kbC5; rat brain [8] and rat liver [24]. Amino acids which are identical between all four isozymes are enclosed in boxes.…”

Section: Discussionmentioning

confidence: 99%

“…Precise mapping of the loci is in progress. Sequencing reinforced this hypothesis as nucleotides 2-215 of 500bC6 are predicted to encode 72 amino acids which show extremely high homology to the 3' ends of rat liver (96% nucleotide, 100% amino acid homology) [24] and human liver (82% nucleotide, 96% amino acid homology) [25] isozyme sequences; the fragment is therefore predicted to encode the mouse homologue (sequence submitted to EMBL/Genbank databases, accession no. X98848).…”

Section: Isolation and Characterization Of Cdna Clonesmentioning

confidence: 91%

See 1 more Smart Citation

Molecular cloning and tissue‐specific expression of mouse kidney 6‐phosphofructo‐2‐kinase/fructose‐2,6‐bisphosphatase

Batra

Brown

et al. 1996

FEBS Letters

View full text Add to dashboard Cite

A 1932 bp cDNA clone encoding a novel isozyme of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/ FBPase-2) was isolated from a mouse kidney cDNA library. The sequence encodes 519 amino acids and, based on homology to rat heart genomic sequence, appears to be the product of alternative splicing from PFK-2/FBPase-2 gene B with an extended version of exon 15. Northern blot analysis indicated that this clone corresponds to an 8 kb mRNA expressed in multiple tissues, with the strongest signal in kidney, and detects several additional transcripts which may be alternatively spliced from gene B.

show abstract

Complete nucleotide sequence coding for rat liver 6‐phosphofructo‐2‐kinase/fructose‐2,6‐bisphosphatase derived from a cDNA clone

Cited by 78 publications

References 19 publications

Transcriptional control of genes that regulate glycolysis and gluconeogenesis in adult liver

Transcriptional control of genes that regulate glycolysis and gluconeogenesis in adult liver

5' flanking sequence and structure of a gene encoding rat 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.

Molecular cloning and tissue‐specific expression of mouse kidney 6‐phosphofructo‐2‐kinase/fructose‐2,6‐bisphosphatase

Contact Info

Product

Resources

About