Lysosomal diacylglycerol pyrophosphate phosphatase is not essential in Trypanosoma brucei.

Dawoody Nejad, Ladan; Annese, Tiziana; Ribatti, Domenico (2024). Lysosomal diacylglycerol pyrophosphate phosphatase is not essential in Trypanosoma brucei. Molecular biology reports, 51(578) Springer 10.1007/s11033-024-09547-w

Text s11033-024-09547-w.pdf - Published Version Restricted to registered users only Available under License Publisher holds Copyright. Download (1MB) | Request a copy

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 β-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.

Interest & Impact

Downloads

0 since deposited on 29 Apr 2024
0 in the past 12 months

Citations

5 Citations in Web of Science ®
6 Citations in Scopus

Search

in Google Scholar™

Services

Actions (login required)

Edit item

Actions (login required)

Edit item