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Published August 11, 1992 | public
Journal Article

The yeast FBP26 gene codes for a fructose-2,6-bisphosphatase

Abstract

Sequencing of an open reading frame 450 bp downstream from the yeast VPS35 gene revealed a putative peptide of 452 amino acids and 52.7 kDa. The predicted amino acid sequence has 45% identity with the 55-kDa subunit of the 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatas(eE C 2.7.1.105/EC 3.1.3.46) from rat liver and 42% identity with 480 amino acids in the center of the recently reported 93.5-kDa subunit of yeast 6-phosphofructo-Zkinase (EC 2.7.1.105). The product of the new yeast gene is similar to the entire sequence of the bifunctional rat liver enzyme and, unlike yeast 6-phosphofructo-2-kinase, has the histidine residue essential for fructose-2,6-bisphosphatase activity. Extracts from a chromosomal null mutant strain, fbp26::HIS3, incubated in the presence of [2-^(32)P]fructose 2,6-P_2, lacked in autoradiograms the characteristic 56-kDa labeled band observed in wild-type. The same band was intensified 3-fold over wild-type level with the FBP26 gene introduced on multicopy in the fbp26::HIS3 background. A similar increase was found for fructose-2,6-bisphosphatasea ctivity in the same extracts. The FBP26 gene did not cause detectable increase in 6-phosphofructo-2-kinasea ctivity when introduced on multicopy in a pfk26::LEU2 mutant, indicating that its gene product is predominantly a fructose-2,6-bisphosphatase. Growth on glucose, fructose, galactose, pyruvate, and glycerol/lactate was not impaired in strains carrying the fbp26::HIS3 allele.

Additional Information

© 1992 American Chemical Society. Published in print 11 August 1992. Supported by the Swiss National Foundation (fellowship to G.P.), by NIH Grant GM 32703 (to Scott Emr), and by NIH Grant GM 21098 (to Dan G. Fraenkel). We thank Scott D. Emr and Dan G. Fraenkel for generous support and criticism.

Additional details

Created:
August 20, 2023
Modified:
October 18, 2023