Molecular analysis of phosphoglycerate kinase in Trypanoplasma borreli and the evolution of this enzyme in kinetoplastida.
In the protozoan kinetoplastid organism Trypanoplasma borreli, phosphoglycerate kinase ( PGK) activity was found in two different cell compartments: 80% in the cytosol and 20% in peroxisome-like organelles called glycosomes. However, only one functional pgk gene could be detected, in addition to a pseudo-pgk gene. No short-range linkage could be established between these two genes, although they are presumably present on the same chromosome. The intact gene codes for a polypeptide of 411 amino acids, with a C-terminal extension of four residues, -VAKF, a sequence with probably a low targeting efficiency for glycosomes. The calculated net charge and molecular mass of the encoded polypeptide are +13 and 44230Da, respectively. In other Kinetoplastida, different tandemly arranged genes code for distinct PGK isoenzymes in glycosomes and cytosol. By comparison of the pgk gene organization, and a phylogenetic analysis, we have traced a plausible scenario of the evolution of the PGK isoenzymes in these organisms and of the enzymes' intracellular compartmentation.[1]References
- Molecular analysis of phosphoglycerate kinase in Trypanoplasma borreli and the evolution of this enzyme in kinetoplastida. Adjé, C.A., Opperdoes, F.R., Michels, P.A. Gene (1998) [Pubmed]
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