The Gup1 homologue of Trypanosoma brucei is a GPI glycosylphosphatidylinositol remodelase
- Jaquenoud, Malika Department of Medicine/Biochemistry, University of Fribourg, Switzerland
- Pagac, Martin Department of Medicine/Biochemistry, University of Fribourg, Switzerland
- Signorell, Aita Institute of Biochemistry and Molecular Medicine, University of Bern, Switzerland
- Benghezal, Mohammed Department of Medicine/Biochemistry, University of Fribourg, Switzerland - Helicobacter Research Laboratory, University of Western Australia, Nedlands, Western Australia
- Jelk, Jennifer Institute of Biochemistry and Molecular Medicine, University of Bern, Switzerland
- Bütikofer, Peter Institute of Biochemistry and Molecular Medicine, University of Bern, Switzerland
- Conzelmann, Andreas Department of Medicine/Biochemistry, University of Fribourg, Switzerland
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07.12.2007
Published in:
- Molecular Microbiology. - 2008, vol. 67, no. 1, p. 202-212
English
Glycosylphosphatidylinositol (GPI) lipids of Trypanosoma brucei undergo lipid remodelling, whereby longer fatty acids on the glycerol are replaced by myristate (C14:0). A similar process occurs on GPI proteins of Saccharomyces cerevisiae where Per1p first deacylates, Gup1p subsequently reacylates the anchor lipid, thus replacing a shorter fatty acid by C26:0. Heterologous expression of the GUP1 homologue of T. brucei in gup1Δ yeast cells partially normalizes the gup1Δ phenotype and restores the transfer of labelled fatty acids from Coenzyme A to lyso-GPI proteins in a newly developed microsomal assay. In this assay, the Gup1p from T. brucei (tbGup1p) strongly prefers C14:0 and C12:0 over C16:0 and C18:0, whereas yeast Gup1p strongly prefers C16:0 and C18:0. This acyl specificity of tbGup1p closely matches the reported specificity of the reacylation of free lyso-GPI lipids in microsomes of T. brucei. Depletion of tbGup1p in trypanosomes by RNAi drastically reduces the rate of myristate incorporation into the sn-2 position of lyso-GPI lipids. Thus, tbGup1p is involved in the addition of myristate to sn-2 during GPI remodelling in T. brucei and can account for the fatty acid specificity of this process. tbGup1p can act on GPI proteins as well as on GPI lipids.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Biologie
- Language
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- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 8877
- DOI 10.1111/j.1365-2958.2007.06043.x
- Persistent URL
- https://folia.unifr.ch/unifr/documents/300683
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