Lysosomal diacylglycerol pyrophosphate phosphatase is not essential in Trypanosoma brucei.
Mol Biol Rep
; 51(1): 578, 2024 Apr 26.
Article
em En
| MEDLINE
| ID: mdl-38668789
ABSTRACT
Mg2+-independent phosphatidic acid phosphatase (PAP2), diacylglycerol pyrophosphate phosphatase 1 (Dpp1) is a membrane-associated enzyme in Saccharomyces cerevisiae. The enzyme is responsible for inducing the breakdown of ß-phosphate from diacylglycerol pyrophosphate (DGPP) into phosphatidate (PA) and then removes the phosphate from PA to give diacylglycerol (DAG). In this study through RNAi suppression, we have demonstrated that Trypanosoma brucei diacylglycerol pyrophosphate phosphatase 1 (TbDpp1) procyclic form production is not required for parasite survival in culture. The steady-state levels of triacylglycerol (TAG), the number of lipid droplets, and the PA content are all maintained constant through the inducible down-regulation of TbDpp1. Furthermore, the localization of C-terminally tagged variants of TbDpp1 in the lysosome was demonstrated by immunofluorescence microscopy.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Trypanosoma brucei brucei
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Glicerol
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Lisossomos
Idioma:
En
Revista:
Mol Biol Rep
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Mol. Biol. reports
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Molecular biology reports
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
Canadá