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Biogenesis of Glycosomes of Trypanosoma Brucei

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Biogenesis of Glycosomes of Trypanosoma Brucei Proc. Natl. Acad. Sci. USA Vol. 85, pp. 2598-2602, April 1988 Cell Biology Biogenesis of glycosomes of Trypanosoma brucei: An in vitro model of 3-phosphoglycerate kinase import (in vitro transcription of cloned DNA/in vitro translation/proteinase K digestion/signal sequence) HARRY F. DOVEY*, MARILYN PARSONSt*, AND CHING C. WANG*§ *Department of Pharmaceutical Chemistry, University of California, School of Pharmacy, San Francisco, CA 94143; tSeattle Biomedical Research Institute, 4 Nickerson Street, Seattle, WA 98109; and tDepartment of Pathobiology, University of Washington, Seattle, WA 98195 Communicated by Y. W. Kan, November 23, 1987 (receivedfor review August 3, 1987) ABSTRACT Glycosomes are intracellular, membrane- ined thus far, in vitro translation ofmRNA yields GPs with the bound microbody organelles of trypanosomes and leishmania. same molecular weights as the mature products inside the Nine glycolytic enzymes are the major protein components of glycosome (6), suggesting that the import may not involve the glycosomes of Trypanosoma brucei long-slender blood- proteolytic processing. Thus, this process appears similar to stream forms. Glycosomal proteins are believed to be synthe- the biogenesis of other microbodies, such as the peroxisomes sized in the cytoplasm and inserted across the glycosomal of yeast and mammals (7-9) and the glyoxysomes of plants membrane posttranslationally. We have developed an in vitro (10), and differs from the biogenesis of mitochondria and protein import assay for the study of glycosomal biogenesis in chloroplasts where posttranslational protein import generally T. brucei. All nine glycosomal glycolytic enzymes were detect- involves proteolytic cleavage of specific leader sequences able by immunoprecipitation and gel analysis of radiolabeled (11-13). products derived from in vitro translation of total mRNA. Studies of glycosome biogenesis in T. brucei have been Radiolabeled translational products were incubated with pu- hampered by the lack of an in vitro protein import assay (8), rified glycosomes isolated from bloodstream forms and di- which has been instrumental to the biochemical analysis of gested with protease to remove proteins not imported into protein transport into mitochondria (13) and chloroplasts glycosomes. Gel analysis of reisolated glycosomes revealed that (14). We have resolved the difficulties in preparing pure glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) and intact glycosomes with reproducible native membrane prop- 3-phosphoglycerate kinase (PGK) (EC 2.7.2.3) were appar- erties. Furthermore, the recent successful cloning and se- ently imported intact into the glycosome. Specificity of the quencing of several glycosomal genes (15-18) have enabled protein import assay was verified by using translational prod- us to use gene clones to generate single gene products and to ucts derived from cloned genes encoding T. brucei glycosomal monitor their import into glycosomes individually. We re- PGK and its 95% homologous cytosolic isozyme. Glycosomal port here the successful development of an in vitro GP PGK was inserted into the glycosome in vitro with a 27.6% dissection of the efficiency, but no imported cytosolic PGK was detectable. import assay, which should allow protein Preliminary data suggest that certain sequences between the N structural requirements for import. terminus and residue 123 may be important for import of glycosomal PGK. Our assay, combined with the potential use MATERIALS AND METHODS of genetically altered substrate proteins, may provide the All chemicals used were obtained from Sigma, unless noted opportunity to explore the recognition systems involved in otherwise, and were of the highest purity available. glycosome biogenesis. Growth and Isolation of T. brucei and Preparation of Glycosomes. The long-slender bloodstream form of T. brucei African trypanosomes in the bloodstream of the infected monomorphic strain EATRO 110 was grown and isolated as mammalian host possess a significant metabolic deficiency- described (19). that is, their mitochondrion contains neither cytochromes For glycosome preparation, trypanosomes were sus- nor a functional tricarboxylic acid cycle (1). Consequently, pended in an equal volume of 25 mM Tris HCI, pH 7.8/1 mM they are dependent entirely on glycolysis for energy. The EDTA/1 mM dithiothreitol/250 mM sucrose (TEDS) with 1 rate of glycolysis in Trypanosoma brucei is 50 times higher ,tM leupeptin and subjected to gentle homogenization by than that in mammalian cells (2). This is apparently made five strokes in a Dounce homogenizer (Kontes) with a possible by confining the first seven glycolytic enzymes and small-clearance pestle (0.025-0.075 mm) at 4°C. Following two glycerol-metabolizing enzymes within glycosomes (3), centrifugation at 1000 x g for 10 min at 4°C, the pelleted which are membrane-bound microbody-like organelles nuclei and unbroken trypanosomes was resuspended and unique to parasites of the order Kinetoplastida. An under- homogenized again as above. This procedure was repeated standing of the mechanism of biogenesis of glycosomes once more. All supernatants were pooled and centrifuged at should be valuable in combating the diseases caused by 5000 x g for 10 min at 4°C to remove the large granular these organisms. fraction. Glycosomes were pelleted by centrifugation at T. brucei glycosomes contain 10% of the total cellular 33,000 x g for 30 min at 4°C and resuspended in TEDS at protein (4) but no nucleic acids (5). It has been assumed that 1-2 mg of protein per ml. This suspension (3-4 ml) was the genes encoding glycosomal proteins (GPs) are located in layered on a 32-ml, 1-2 M linear sucrose gradient in TEDS the nucleus and the products of these genes are synthesized and centrifuged at 49,000 rpm for 90 min at 4°C in a VTi-50 in the cytoplasm on free polysomes (6). Thus, glycosome rotor in a Beckman L8-80M ultracentrifuge. The lower, assembly would require insertion of proteins across the prominent band was collected (p = 1.23 g/cm3) (19), diluted organelle membrane posttranslationally. In the cases exam- Abbreviations: PGK, 3-phosphoglycerate kinase; g-, glycosomal; c-, The publication costs of this article were defrayed in part by page charge cytosolic; PhMeSO2F, phenylmethylsulfonyl fluoride; GP, glyco- payment. This article must therefore be hereby marked "advertisement" somal protein. in accordance with 18 U.S.C. §1734 solely to indicate this fact. §To whom reprint requests should be addressed. Downloaded by guest on October 2, 2021 2598 Cell Biology: Dovey et A Proc. Natl. Acad. Sci. USA 85 (1988) 2599 1:5 with TEDS, and pelleted by centrifugation at 33,000 x g isozyme-specific oligonucleotide probes, the position of the for 30 min at 4°C. Purified glycosomes, resuspended in gene in the cluster, restriction enzyme mapping, and analysis TEDS to a final concentration of 1 mg/ml, were stored at of the protein products encoded by the gene. - 700C. The coding regions of the genes, plus a small amount of 5' Antibody Preparation and Immunoprecipitation. Polyclo- flanking sequences, were subcloned into pBS (Stratagene, nal antiserum to total GP (anti-GP) was raised in rabbits by San Diego, CA), a plasmid vector that contains the T3 and using an initial intradermal injection of 0.75 mg of purified T7 promoters on either side of the polylinker cloning site. glycosomes in Freund's complete adjuvant and several The c-PGK subclone, 123-2, contains 170 base pairs (bp) of booster injections at 2-week intervals with 0.75 mg of antigen 5' noncoding sequence, whereas the g-PGK subclone, 44-1, in Freund's incomplete adjuvant. Reactivity to the variant contains 50 bp of the flanking region. In both cases, the first surface glycoprotein was removed by absorption on a con- ATG codon starts the authentic protein. The plasmids were canavalin A-agarose column previously saturated with the linearized, and transcripts were synthesized in vitro by using variant surface glycoprotein. Anti-GP was examined by T3 or T7 RNA polymerase (Stratagene) according to the immunoblotting experiments (20) and found to react specif- orientation of the gene. ically with the nine glycolytic enzymes in the purified In Vitro Translation and GP Import Assay. RNAs were glycosomes. translated in a cell-free protein synthesizing system (nucle- A 22-amino acid peptide, composed of an N-terminal ase-treated rabbit reticulocyte lysate, Promega Biotec, Mad- cysteine plus the C-terminal 21 amino acids of glycosomal ison, WI) containing 1 ttCi (1 Ci = 37 GBq) of [35S]methi- 3-phosphoglycerate kinase (EC 2.7.2.3; g-PGK), designated onine per Al (New England Nuclear, >800 Ci/mmol) for 60 C-22, was synthesized by the Biomedical Resource Center, min at 30'C. Typically 1 Ag of RNA in a 50-pl reaction University of California, San Francisco, with an Applied volume yielded 2-3 x 105 cpm/,l (for T. brucei mRNA) or Biosystem 430A peptide synthesizer and purified by C18 4-8 x 104 cpm/,ul (for uncapped g-PGK or c-PGK gene ODS reversed-phase HPLC. The final structure was con- transcripts) as trichloroacetic acid-precipitable protein. Im- firmed by peptide sequencing: H2N-Cys-Ser-Ala-Val-Val- mediately following this incubation, 2 M sucrose/25 mM Ser-Tyr-Ala-Ser-Ala-Gly-Thr-Gly-Thr-Leu-Ser-Asn-Arg- Tris-HCI, pH 7.8/1 mM EDTA/1 mM dithiothreitol was Trp-Ser-Ser-Leu-CO2H (16). Antiserum to this peptide (anti- added to yield a final concentration of 250 mM sucrose. C-22) was prepared in a manner similar to that described Glycosomes at 0.4 mg of protein per ml in 240 Al of TEDS above, except that initial immunizations of 1 mg, followed by with 10 mM methionine/1 mM ATP/5 mM phospho- 0.5-mg booster injections, were used. The N-terminal cys- enolpyruvate/2 mM MgCI2/4 units of pyruvate kinase per ml teine was originally added to the peptide to couple it to a were mixed with 10 ,ul of the translation mixture and carrier protein for the purpose of immunization.
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