Characterization of the genes for fructose-bisphosphate aldolase in Trypanosoma brucei.
(1988) Molecular and Biochemical Parasitology — Vol. 29, n° 1, p. 65-75 (1988)
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- In Trypanosoma brucei stock 427 the glycolytic enzyme fructose-bisphosphate aldolase is encoded by two tandemly linked genes of identical sequence. Such a tandem arrangement of aldolase genes is also present in other T. brucei stocks of unrelated origin. In stock 427 one of the allelic genes is a pseudogene, as a result of a one-nucleotide deletion. The genes code for a polypeptide of 371 amino acids, with a calculated molecular weight of 40,940. The protein that is predicted from the gene sequence has 45-48% positional identity with known aldolase sequences of other organisms. The trypanosomal protein is, however, unique in having a 10 amino-acid insertion near its N-terminus and high number of basic residues, a feature it shares with other glycolytic enzymes of T. brucei. These glycolytic enzymes have in common that they are located in microbody-like organelles, the glycosomes. We have previously proposed that the positively charged residues may be involved in the import of the proteins into the organelles.
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Marchand, M., Poliszczak, A., Gibson, W. C., Wierenga, R. K., Opperdoes, F., & Michels, P. (1988). Characterization of the genes for fructose-bisphosphate aldolase in Trypanosoma brucei. Molecular and Biochemical Parasitology, 29(1), 65-75. https://doi.org/10.1016/0166-6851(88)90121-1 (Original work published 1988)