A phosphoglycerate kinase-like molecule localized to glycosomal microbodies: evidence that the topogenic signal is not at the C-terminus

Alexander, Kenneth R.; Parsons, Marilyn

doi:10.1016/0166-6851(91)90193-a

Cited by 30 publications

(9 citation statements)

References 26 publications

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“…Immunodetection was performed as described (37,38) using as primary antibodies rabbit anti-PGK (diluted 1:500; gift from P. Michels, Edinburgh, UK, and M. Parsons, Seattle, WA) (39,40), rat anti-PEPCK (diluted 1:1000; gift from T. Seebeck, Bern, Switzerland) (22), rabbit anti-PPDK (diluted 1:500) (5), rabbit anti-TDH (diluted 1:500) (11), rabbit anti-GPDH (glycerol-3-phosphate dehydrogenase, EC 1.1.1.8; diluted 1:100) (41), mouse anti-hsp60 (diluted 1:10,000) (42), and mouse anti-AMP-dependent acetyl-CoA synthetase (EC 6.2.1.1; diluted 1:100) (43) and as secondary antibodies, anti-mouse, anti-rat, or anti-rabbit IgG conjugated to horseradish peroxidase (Bio-Rad, 1:5,000 dilution). Revelation was performed using the SuperSignal West Pico Chemiluminescent Substrate as described by the manufacturer (Thermo Scientific).…”

Section: Methodsmentioning

confidence: 99%

Contribution of Pyruvate Phosphate Dikinase in the Maintenance of the Glycosomal ATP/ADP Balance in the Trypanosoma brucei Procyclic Form

Deramchia

Morand

Biran

et al. 2014

Journal of Biological Chemistry

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Background:The role of pyruvate phosphate dikinase (PPDK), which catalyzes a reversible reaction, is unknown in many eukaryotes. Results: Deletion of the trypanosomal PPDK gene affects glycolysis. Conclusion:In trypanosomes, PPDK works in the glycolytic direction and participates in the maintenance of the glycosomal ATP/ADP balance. Significance: The glycosomal PPDK provides a metabolic flexibility by producing 2 ATP per phosphoenolpyruvate consumed.

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Section: Methodsmentioning

confidence: 99%

Contribution of Pyruvate Phosphate Dikinase in the Maintenance of the Glycosomal ATP/ADP Balance in the Trypanosoma brucei Procyclic Form

Deramchia

Morand

Biran

et al. 2014

Journal of Biological Chemistry

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“…These are highly similar and must have originated through gene duplication, followed by gene conversions partially erasing differences that arose by genetic drift (Le Blancq et al 1988;Alexander and Parsons 1991;Swinkels et al 1992). Therefore, PGK is not very informative concerning the organelle origin.…”

Section: Introductionmentioning

confidence: 99%

Molecular analysis of glyceraldehyde-3-phosphate dehydrogenase in Trypanoplasma borelli: An evolutionary scenario of subcellular compartmentation in Kinetoplastida

et al. 1995

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In Trypanoplasma borelli, a representative of the Bodonina within the Kinetoplastida, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) activity was detected in both the cytosol and glycosomes. This situation is similar to that previously found in Trypanosomatidae, belonging to a different Kinetoplastida suborder. In Trypanosomatidae different isoenzymes, only distantly related, are responsible for the activity in the two cell compartments. In contrast, immunoblot analysis indicated that the GAPDH activity in cytosol and glycosomes of T. borelli should be attributed to identical or at least very similar proteins related to the glycosomal GAPDH of Trypanosomatidae. Moreover, only genes related to the glycosomal GAPDH genes of Trypanosomatidae could be detected. All attempts to identify a gene related to the one coding for the trypanosomatid cytosolic GAPDH remained unsuccessful. Two tandemly arranged genes were found which are 95% identical. The two encoded polypeptides differ in 17 residues. Their sequences are 72-77% identical to the glycosomal GAPDH of the other Kinetoplastida and share with them some characteristic features: an excess of positively charged residues, specific insertions, and a small carboxy-terminal extension containing the sequence -AKL. This tripeptide conforms to the consensus signal for targeting of proteins to glycosomes. One of the two gene copies has undergone some mutations at positions coding for highly conserved residues of the active site and the NAD(+)-binding domain of GAPDH. Modeling of the protein's three-dimensional structure suggested that several of the substitutions compensate each other, retaining the functional coenzyme-binding capacity, although this binding may be less tight. The presented analysis of GAPDH in T. borelli gives further support to the assertion that one isoenzyme, the cytosolic one, was acquired by horizontal gene transfer during the evolution of the Kinetoplastida, in the lineage leading to the suborder Trypanosomatina (Trypanosoma, Leishmania), after the divergence from the Bodonina (Trypanoplasma). Furthermore, the data clearly suggest that the original GAPDH of the Kinetoplastida has been compartmentalized during evolution.

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“…African trypanosomes have three genes encoding phosphoglycerate kinase (PGK) (12,28). One (PGK-B) is a cyto-plasmic PGK, and another (PGK-A) is a minor glycosomal enzyme that has an internal 80-amino acid insertion relative to the cytoplasmic PGK (2,22,36). The third PGK (PGK-C) is the major glycosomal enzyme.…”

mentioning

confidence: 99%

Glycosome assembly in trypanosomes: variations in the acceptable degeneracy of a COOH-terminal microbody targeting signal.

Blattner¹,

Swinkels²,

Dörsam³

et al. 1992

The Journal of Cell Biology

114

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A phosphoglycerate kinase-like molecule localized to glycosomal microbodies: evidence that the topogenic signal is not at the C-terminus

Cited by 30 publications

References 26 publications

Contribution of Pyruvate Phosphate Dikinase in the Maintenance of the Glycosomal ATP/ADP Balance in the Trypanosoma brucei Procyclic Form

Contribution of Pyruvate Phosphate Dikinase in the Maintenance of the Glycosomal ATP/ADP Balance in the Trypanosoma brucei Procyclic Form

Molecular analysis of glyceraldehyde-3-phosphate dehydrogenase in Trypanoplasma borelli: An evolutionary scenario of subcellular compartmentation in Kinetoplastida

Glycosome assembly in trypanosomes: variations in the acceptable degeneracy of a COOH-terminal microbody targeting signal.

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