Characterization of key enzymes involved in triacylglycerol biosynthesis in mycobacteria

dc.citation.titleNature Researches
dc.citation.volume11es
dc.creatorCrotta Asis, Agostina
dc.creatorSavoretti, Franco
dc.creatorCabruja, Matías Ezequiel
dc.creatorGramajo, Hugo Cesar
dc.creatorGago, Gabriela
dc.date.accessioned2022-03-28T21:44:41Z
dc.date.available2022-03-28T21:44:41Z
dc.date.issued2021-06-24
dc.descriptionPhosphatidic 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.es
dc.description.filFil: CrottaAsis, Agostina. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET). Argentina.es
dc.description.filFil: Savoretti, Franco. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET). Argentina.es
dc.description.filFil: Cabruja, Matías Ezequiel. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET). Argentina.es
dc.description.filFil: Gramajo, Hugo Cesar. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET). Argentina.es
dc.description.filFil: Gago, Gabriela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET). Argentina.es
dc.description.sponsorshipAgencia Nacional de Promoción de la Investigación, el Desarrollo Tecnológico y la Innovación
dc.description.sponsorshipAgencia Nacional de Promoción Científica y Tecnológica (ANPCyT): 2015-0796, 2015-2022, 2018-02539
dc.formatapplication/pdf
dc.format.extent1-13es
dc.identifier.issn2045-2322es
dc.identifier.urihttp://hdl.handle.net/2133/23274
dc.language.isoenges
dc.publisherScientific Reportses
dc.relation.publisherversionhttps://www.nature.com/articles/s41598-021-92721-y#additional-informationes
dc.relation.publisherversionhttps://doi.org/10.1038/s41598-021-92721-y
dc.rightsopenAccesses
dc.rights.holderCrotta Asis, Agostinaes
dc.rights.holderSavoretti, Francoes
dc.rights.holderCabruja, Matías Ezequieles
dc.rights.holderGramajo, Hugpo Cesares
dc.rights.holderGago, Gabrielaes
dc.rights.textAttribution 4.0 International (CCBY4.0)es
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/deed.es*
dc.subjectEscherichia Colies
dc.subjectLipid Metabolismes
dc.subjectMycobacterium Smegmatises
dc.subjectPhosphatidate Phosphatasees
dc.subjectPhosphatidic Acidses
dc.subjectPhylogenyes
dc.subjectTriglycerideses
dc.titleCharacterization of key enzymes involved in triacylglycerol biosynthesis in mycobacteriaes
dc.typepublishedVersion
dc.typearticle
dc.typeartículo
dc.type.collectionarticulo
dc.type.versionpublishedVersion

Archivos

Bloque original
Mostrando 1 - 1 de 1
Cargando...
Miniatura
Nombre:
Characterization of key enzymes.pdf
Tamaño:
2.29 MB
Formato:
Adobe Portable Document Format
Descripción:
Bloque de licencias
Mostrando 1 - 1 de 1
Nombre:
license.txt
Tamaño:
3.59 KB
Formato:
Item-specific license agreed upon to submission
Descripción: