S.J. Suzuki, M.A. Mutton, J.M. Pizauro, M. I.T. Ferro, M. V.F. Lemos, M. J.R. Mutton, S. M.Z. Di Mauro
Published: December 30, 2003
Genet. Mol. Res. 2 (4) : 376-382
Cite this Article:
S.J. Suzuki, M.A. Mutton, J.M. Pizauro, M.I.T. Ferro, M.V.F. Lemos, M.J.R. Mutton, S.M.Z. Di Mauro (2003). Putative pyrophosphate phosphofructose 1-kinase genes identified in sugar cane may be getting energy from pyrophosphate. Genet. Mol. Res. 2(4): 376-382.
About the Authors
S.J. Suzuki, M.A. Mutton, J.M. Pizauro, M. I.T. Ferro, M. V.F. Lemos, M. J.R. Mutton, S. M.Z. Di Mauro
Corresponding author
M.J.R. Muton
E-mail: mjrmut@facav.unesp.br
ABSTRACT
Pyrophosphate-dependent phosphofructokinase (PPi-PFK) has been detected in several types of plant cells, but the gene has not been reported in sugar cane. Using Citrus paradisi PPi-PFK gene (AF095520 and AF095521) sequences to search the sugar cane EST database, we have identified both the α and β subunits of this enzyme. The deduced amino acid sequences showed 76 and 80% similarity with the corresponding α and β subunits of C. paradisi. A high degree of similarity was also observed among the PFK β subunits when the alignment of the sugar cane sequences was compared to those of Ricinus communis and Solanum tuberosum. It appears that α and β are two distinct subunits; they were found at different concentrations in several sugar cane tissues. It remains to be determined if the different gene expression levels have some physiological importance and how they affect sucrose synthesis, export, and storage in vacuoles. A comparison between the amino acid sequences of β PFKs from a variety of organisms allowed us to identify the two critical Asp residues typical of this enzyme’s activity site and the other binding sites; these residues are tightly conserved in all members of this protein family. Apparently, there are catalytic residues on the β subunit of the pyrophosphate-dependent enzyme.
Key words: Pyrophosphate phosphofructose 1-kinase, Sugar cane, ATP, Sucrose, Sucrose synthase, PPi-PFK.