Characterization of key enzymes involved in triacylglycerol biosynthesis in mycobacteria

Phosphatidic acid phosphatase (PAP) catalyzes the dephosphorylation of phosphatidic acid (PA) yielding diacylglycerol (DAG), the lipid precursor for triacylglycerol (TAG) biosynthesis. PAP activity has a key role in the regulation of PA flux towards TAG or glycerophospholipid synthesis. In this work...

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Detalles Bibliográficos
Autores principales: Crotta Asis, Agostina, Savoretti, Franco, Cabruja, Matías Exequiel, Gramajo, Hugo Cesar, Gago, Gabriela
Formato: article artículo publishedVersion
Lenguaje:Inglés
Publicado: Scientific Reports 2022
Materias:
Escherichia Coli
Lipid Metabolism
Mycobacterium Smegmatis
Phosphatidate Phosphatase
Phosphatidic Acids
Phylogeny
Triglycerides
Acceso en línea:http://hdl.handle.net/2133/23274
http://hdl.handle.net/2133/23274
Aporte de:
Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR) de Universidad Nacional de Rosario
id I15-R121-2133-23274
record_format dspace
institution Universidad Nacional de Rosario
institution_str I-15
repository_str R-121
collection Repositorio Hipermedial de la Universidad Nacional de Rosario (UNR)
language Inglés
orig_language_str_mv eng
topic Escherichia Coli
Lipid Metabolism
Mycobacterium Smegmatis
Phosphatidate Phosphatase
Phosphatidic Acids
Phylogeny
Triglycerides
spellingShingle Escherichia Coli
Lipid Metabolism
Mycobacterium Smegmatis
Phosphatidate Phosphatase
Phosphatidic Acids
Phylogeny
Triglycerides
Crotta Asis, Agostina
Savoretti, Franco
Cabruja, Matías Exequiel
Gramajo, Hugo Cesar
Gago, Gabriela
Characterization of key enzymes involved in triacylglycerol biosynthesis in mycobacteria
topic_facet Escherichia Coli
Lipid Metabolism
Mycobacterium Smegmatis
Phosphatidate Phosphatase
Phosphatidic Acids
Phylogeny
Triglycerides
description Phosphatidic acid phosphatase (PAP) catalyzes the dephosphorylation of phosphatidic acid (PA) yielding diacylglycerol (DAG), the lipid precursor for triacylglycerol (TAG) biosynthesis. PAP activity has a key role in the regulation of PA flux towards TAG or glycerophospholipid synthesis. In this work we have characterized two Mycobacterium smegmatis genes encoding for functional PAP proteins. Disruption of both genes provoked a sharp reduction in de novo TAG biosynthesis in early growth phase cultures under stress conditions. In vivo labeling experiments demonstrated that TAG biosynthesis was restored in the ∆PAP mutant when bacteria reached exponential growth phase, with a concomitant reduction of phospholipid synthesis. In addition, comparative lipidomic analysis showed that the ∆PAP strain had increased levels of odd chain fatty acids esterified into TAGs, suggesting that the absence of PAP activity triggered other rearrangements of lipid metabolism, like phospholipid recycling, in order to maintain the wild type levels of TAG. Finally, the lipid changes observed in the ∆PAP mutant led to defective biofilm formation. Understanding the interaction between TAG synthesis and the lipid composition of mycobacterial cell envelope is a key step to better understand how lipid homeostasis is regulated during Mycobacterium tuberculosis infection.
format article
artículo
publishedVersion
author Crotta Asis, Agostina
Savoretti, Franco
Cabruja, Matías Exequiel
Gramajo, Hugo Cesar
Gago, Gabriela
author_facet Crotta Asis, Agostina
Savoretti, Franco
Cabruja, Matías Exequiel
Gramajo, Hugo Cesar
Gago, Gabriela
author_sort Crotta Asis, Agostina
title Characterization of key enzymes involved in triacylglycerol biosynthesis in mycobacteria
title_short Characterization of key enzymes involved in triacylglycerol biosynthesis in mycobacteria
title_full Characterization of key enzymes involved in triacylglycerol biosynthesis in mycobacteria
title_fullStr Characterization of key enzymes involved in triacylglycerol biosynthesis in mycobacteria
title_full_unstemmed Characterization of key enzymes involved in triacylglycerol biosynthesis in mycobacteria
title_sort characterization of key enzymes involved in triacylglycerol biosynthesis in mycobacteria
publisher Scientific Reports
publishDate 2022
url http://hdl.handle.net/2133/23274
http://hdl.handle.net/2133/23274
work_keys_str_mv AT crottaasisagostina characterizationofkeyenzymesinvolvedintriacylglycerolbiosynthesisinmycobacteria
AT savorettifranco characterizationofkeyenzymesinvolvedintriacylglycerolbiosynthesisinmycobacteria
AT cabrujamatiasexequiel characterizationofkeyenzymesinvolvedintriacylglycerolbiosynthesisinmycobacteria
AT gramajohugocesar characterizationofkeyenzymesinvolvedintriacylglycerolbiosynthesisinmycobacteria
AT gagogabriela characterizationofkeyenzymesinvolvedintriacylglycerolbiosynthesisinmycobacteria
bdutipo_str Repositorios
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