Molecular analysis of phosphoglycerate kinase in Trypanoplasma borreli and the evolution of this enzyme in kinetoplastida.
(1998) Gene — Vol. 217, n° 1-2, p. 91-99 (1998)
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- 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.
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Adjé, C. A., Opperdoes, F., & Michels, P. (1998). Molecular analysis of phosphoglycerate kinase in Trypanoplasma borreli and the evolution of this enzyme in kinetoplastida. Gene, 217(1-2), 91-99. https://doi.org/10.1016/S0378-1119(98)00356-4 (Original work published 1998)