Unravelling the lipoyl-relay of exogenous lipoate utilization in Bacillus subtilis

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dc.citation.titleMolecular Microbiology
dc.citation.volume112
dc.contributor.orcidhttps://orcid.org/0000-0002-1444-8661
dc.creatorRasetto, Natalí B.
dc.creatorLavatelli, Antonela
dc.creatorMartin, Natalia
dc.creatorMansilla, María Cecilia
dc.date.accessioned2024-12-10T16:56:24Z
dc.date.available2024-12-10T16:56:24Z
dc.date.issued2019-05-19
dc.description.abstractLipoate is an essential cofactor for key enzymes of oxidative and one-carbon metabolism. It is covalently attached to E2 subunits of dehydrogenase complexes and GcvH, the H subunit of the glycine cleavage system. Bacillus subtilis possess two protein lipoylation pathways: biosynthesis and scavenging. The former requires octanoylation of GcvH, insertion of sulfur atoms and amidotransfer of the lipoate to E2s, catalyzed by LipL. Lipoate scavenging is mediated by a lipoyl protein ligase (LplJ) that catalyzes a classical two-step ATP-dependent reaction. Although these pathways were thought to be redundant, a ∆lipL mutant, in which the endogenous lipoylation pathway of E2 subunits is blocked, showed growth defects in minimal media even when supplemented with lipoate and despite the presence of a functional LplJ. In this study, we demonstrate that LipL is essential to modify E2 subunits of branched chain ketoacid and pyruvate dehydrogenases during lipoate scavenging. The crucial role of LipL during lipoate utilization relies on the strict substrate specificity of LplJ, determined by charge complementarity between the ligase and the lipoylable subunits. This new lipoyl-relay required for lipoate scavenging highlights the relevance of the amidotransferase as a valid target for the design of new antimicrobial agents among Gram-positive pathogens.
dc.description.filFil: Rasetto, Natalí B. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.description.filFil: Lavatelli, Antonela. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Departamento de Microbiología. Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET); Argentina.
dc.description.filFil: Martin, Natalia. Michigan State University. Department of Microbiology and MolecularGenetics; USA.
dc.description.filFil: Mansilla, María Cecilia. Michigan State University. Department of Microbiology and MolecularGenetics; USA.
dc.description.sponsorshipAgencia Nacional de Promoción Científica y Tecnológica: PICT 2012-1341
dc.description.sponsorshipConsejo Nacional de Investigaciones Científicas y Técnicas: P-UE 2016-IBR
dc.description.sponsorshipMinisterio de Ciencia, Tecnología e Innovación Productiva: EULACH 16/T02-0161
dc.format.extent302–316
dc.identifier.citationRasetto, Natalí Belén; Lavatelli, Antonela; Martin, Natalia; Mansilla, Maria Cecilia; Unravelling the lipoyl‐relay of exogenous lipoate utilization in Bacillus subtilis; Wiley Blackwell Publishing, Inc; Molecular Microbiology; 112; 1; 5-2019; 302-316
dc.identifier.issn0950-382X
dc.identifier.urihttps://hdl.handle.net/2133/28366
dc.language.isoen
dc.publisherWiley
dc.relation.publisherversionhttps://onlinelibrary.wiley.com/doi/epdf/10.1111/mmi.14271
dc.relation.publisherversionhttps://doi.org/10.1111/mmi.14271
dc.rightsopenAccess
dc.rights.holderJohn Wiley & Sons Ltd
dc.rights.holderUniversidad Nacional de Rosario
dc.rights.textAttribution-NonCommercial-NoDerivatives 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectGlycine decarboxylase complex h-protein
dc.subjectBacillus subtilis
dc.subjectLipoylation
dc.subjectLigases
dc.titleUnravelling the lipoyl-relay of exogenous lipoate utilization in Bacillus subtilis
dc.typearticulo
dc.type.versionpublishedVersion

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