Import of fructose bisphosphate aldolase into the glycosomes of Trypanosoma brucei.
The glycolytic enzymes of Trypanosomatids are compartmentalized within peroxisome-like microbodies called glycosomes. Fructose bisphosphate aldolase is synthesized on free polysomes and imported into glycosomes within 5 min. Peptide mapping reveals no primary structural differences between the in vivo-synthesized protein and that made in vitro from a synthetic template. However, native aldolase from glycosomes is partially protease resistant, whereas the in vitro translation product is not. Pulse-chase results indicate that aldolase in bloodstream trypanosomes has a much longer half-life than in the procyclic tsetse fly form.
Clayton
C E
CE
Rockefeller University, New York 10021-6399.
D000818:Animals; D002458:Cell Fractionation; D003001:Cloning, Molecular; D005634:Fructose-Bisphosphate Aldolase / Q000235:genetics* / Q000378:metabolism; D007700:Kinetics; D008830:Microbodies / Q000201:enzymology* / Q000648:ultrastructure; D010447:Peptide Hydrolases; D010449:Peptide Mapping; D011132:Polyribosomes / Q000201:enzymology; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D014158:Transcription, Genetic; D014346:Trypanosoma brucei brucei / Q000201:enzymology*
D010447:Peptide Hydrolases; D005634:Fructose-Bisphosphate Aldolase