A role for the dynamic acylation of a cluster of cysteine residues in regulating the activity of the glycosylphosphatidylinositol-specific phospholipase C of Trypanosoma brucei.

A role for the dynamic acylation of a cluster of cysteine residues in regulating the activity of the glycosylphosphatidylinositol-specific phospholipase C of Trypanosoma brucei. Research Abstract Details 

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A role for the dynamic acylation of a cluster of cysteine residues in regulating the activity of the glycosylphosphatidylinositol-specific phospholipase C of Trypanosoma brucei. Abstract Text:

F Paturiaux-Hanocq,J Hanocq-Quertier,M L de Almeida,D P Nolan,A Pays,L Vanhamme,J Van den Abbeele,C L Wasunna,M Carrington,E Pays,

The glycosylphosphatidylinositol-specific phospholipase C or VSG lipase is the enzyme responsible for the cleavage of the glycosylphosphatidylinositol anchor of the variant surface glycoprotein (VSG) and concomitant release of the surface coat in Trypanosoma brucei during osmotic shock or extracellular acidic stress. In Xenopus laevis oocytes the VSG lipase was expressed as a nonacylated and a thioacylated form. This thioacylation occurred within a cluster of three cysteine residues but was not essential for catalytic activity per se. These two forms were also detected in trypanosomes and appeared to be present at roughly equivalent amounts. A reversible shift to the acylated form occurred when cells were triggered to release the VSG by either nonlytic acid stress or osmotic lysis. A wild type VSG lipase or a gene mutated in the three codons for the acylated cysteines were reinserted in the genome of a trypanosome null mutant for this gene. A comparative analysis of these revertant trypanosomes indicated that thioacylation might be involved in regulating enzyme access to the VSG substrate.

A role for the dynamic acylation of a cluster of cysteine residues in regulating the activity of the glycosylphosphatidylinositol-specific phospholipase C of Trypanosoma brucei. Publishing Authors By Initials

F Paturiaux-Hanocq,J Hanocq-Quertier,ML de Almeida,DP Nolan,A Pays,L Vanhamme,J Van den Abbeele,CL Wasunna,M Carrington,E Pays,

For similar animals: chordata: vertebrates: amphibia: anura: pipidae: xenopus: xenopus laevis research abstracts see: animals: chordata: vertebrates: amphibia: anura: pipidae: xenopus: xenopus laevis research

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A role for the dynamic acylation of a cluster of cysteine residues in regulating the activity of the glycosylphosphatidylinositol-specific phospholipase C of Trypanosoma brucei. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 275

Page Numbers: 12147-55

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 21

MONTH: Apr

YEAR: 2000

A role for the dynamic acylation of a cluster of cysteine residues in regulating the activity of the glycosylphosphatidylinositol-specific phospholipase C of Trypanosoma brucei. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

A role for the dynamic acylation of a cluster of cysteine residues in regulating the activity of the glycosylphosphatidylinositol-specific phospholipase C of Trypanosoma brucei. Keywords Mesh Terms:

KEYWORDS: Xenopus laevis

MESH TERMS: metabolism

Chemical & Substance for Abstract: A role for the dynamic acylation of a cluster of cysteine residues in regulating the activity of the glycosylphosphatidylinositol-specific phospholipase C of Trypanosoma brucei. Information

Substance Name: Glycosylphosphatidylinositol Diacylglyce

Registry Number: EC 4.6.1.14

Grant and Affiliation Information for A role for the dynamic acylation of a cluster of cysteine residues in regulating the activity of the glycosylphosphatidylinositol-specific phospholipase C of Trypanosoma brucei.

AFFILIATION: Department of Molecular Biology, Université Libre de Bruxelles, 12 rue des Profs Jeener et Brachet, B-6041, Gosselies, Belgium.

Country: UNITED STATES

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MEDLINETA: J Biol Chem

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