(FBIOyF) Departamento de Microbiología - Artículos
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Examinando (FBIOyF) Departamento de Microbiología - Artículos por Autor "Albanesi, Daniela"
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Ítem Acceso Abierto A coiled coil switch mediates cold sensing by the thermosensory protein DesK(Wiley, 2015-10-08) Saita, Emilio Adolfo; Abriata, Luciano Andrés; Tsai, Yi-Ting; Trajtenberg, Felipe; Lemmin, Thomas; Buschiazzo, Alejandro; Dal Peraro, Matteo; De Mendoza, Diego; Albanesi, DanielaThe thermosensor histidine kinase DesK from Bacillus subtilis senses changes in membrane fluidity initiating an adaptive response. Structural changes in DesK have been implicated in transmembrane signaling, but direct evidence is still lacking. On the basis of structure-guided mutagenesis, we now propose a mechanism of DesK-mediated signal sensing and transduction. The data indicate that stabilization/destabilization of a 2-helix coiled coil, which connects the transmembrane sensory domain of DesK to its cytosolic catalytic region, is crucial to control its signaling state. Computational modeling and simulations reveal couplings between protein, water and membrane mechanics. We propose that membrane thickening is the main driving force for signal sensing and that it acts by inducing helix stretching and rotation prompting an asymmetric kinase-competent state. Overall, the known structural changes of the sensor kinase, as well as further dynamic rearrangements that we now predict, consistently link structure determinants to activity modulation.Ítem Acceso Abierto Corrigendum: Identification of novel thermosensors in gram-positive pathogens(2022-08-31) Fernández, Pilar; Díaz, Alejandra Raquel; Ré, María Florencia; Porrini, Lucía; De Mendoza, Diego; Albanesi, Daniela; Mansilla, María CeciliaÍtem Acceso Abierto Identification of Novel Thermosensors in Gram-Positive Pathogens(Frontiers Media, 2020-11-26) Fernández, Pilar; Díaz, Alejandra Raquel; Ré, María Florencia; Porrini, Lucía; De Mendoza, Diego; Albanesi, Daniela; Mansilla, María CeciliaÍtem Acceso Abierto Revisiting the coupling of fatty acid to phospholipid synthesis in bacteria with FapR regulation(Wiley, 2020-07-16) Machinandiarena, Federico; Nakamatsu, Leandro; Schujman, Gustavo Enrique; De Mendoza, Diego; Albanesi, Daniela; https://orcid.org/0000-0003-4380-9152A key aspect in membrane biogenesis is the coordination of fatty acid to phospholipid synthesis rates. In most bacteria, PlsX is the first enzyme of the phosphatidic acid synthesis pathway, the common precursor of all phospholipids. Previously, we proposed that PlsX is a key regulatory point that synchronizes the fatty acid synthase II with phospholipid synthesis in Bacillus subtilis. However, understanding the basis of such coordination mechanism remained a challenge in Gram-positive bacteria. Here, we show that the inhibition of fatty acid and phospholipid synthesis caused by PlsX depletion leads to the accumulation of long-chain acyl-ACPs, the end products of the fatty acid synthase II. Hydrolysis of the acyl-ACP pool by heterologous expression of a cytosolic thioesterase relieves the inhibition of fatty acid synthesis, indicating that acyl-ACPs are feedback inhibitors of this metabolic route. Unexpectedly, inactivation of PlsX triggers a large increase of malonyl-CoA leading to induction of the fap regulon. This finding discards the hypothesis, proposed for B. subtilis and extended to other Gram-positive bacteria, that acyl-ACPs are feedback inhibitors of the acetyl-CoA carboxylase. Finally, we propose that the continuous production of malonyl-CoA during phospholipid synthesis inhibition provides an additional mechanism for fine-tuning the coupling between phospholipid and fatty acid production in bacteria with FapR regulation.Ítem Acceso Abierto The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3(Nature Research, 2022-03-12) Steimbrüch, Bruno A.; Sartorio, Mariana Gabriela; Cortez, Néstor; Albanesi, Daniela; Lisa, María Natalia; Repizo, Guillermo DanielÍtem Acceso Abierto The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis(American Society for Biochemistry and Molecular Biology, 2020-01-09) Sastre, Diego Emiliano; Pulschen, André A.; Basso , Luis G.M.; Benites Pariente, Jhonathan S.; Marques Netto, Caterina G.C.; Machinandiarena, Federico; Albanesi, Daniela; Navarro, Marcos V.A.S.; De Mendoza, Diego; Gueiros-Filho, Frederico J.PlsX is the first enzyme in the pathway that produces phosphatidic acid in Gram-positive bacteria. It makes acylphosphate from acyl-acyl carrier protein (acyl-ACP) and is also involved in coordinating phospholipid and fatty acid biosyntheses. PlsX is a peripheral membrane enzyme in Bacillus subtilis, but how it associates with the membrane remains largely unknown. In the present study, using fluorescence microscopy, liposome sedimentation, differential scanning calorimetry, and acyltransferase assays, we determined that PlsX binds directly to lipid bilayers and identified its membrane anchoring moiety, consisting of a hydrophobic loop located at the tip of two amphipathic dimerization helices. To establish the role of the membrane association of PlsX in acylphosphate synthesis and in the flux through the phosphatidic acid pathway, we then created mutations and gene fusions that prevent PlsX's interaction with the membrane. Interestingly, phospholipid synthesis was severely hampered in cells in which PlsX was detached from the membrane, and results from metabolic labeling indicated that these cells accumulated free fatty acids. Because the same mutations did not affect PlsX transacylase activity, we conclude that membrane association is required for the proper delivery of PlsX's product to PlsY, the next enzyme in the phosphatidic acid pathway. We conclude that PlsX plays a dual role in phospholipid synthesis, acting both as a catalyst and as a chaperone protein that mediates substrate channeling into the pathway.Ítem Acceso Abierto Transmembrane prolines mediate signal sensing and decoding in Bacillus subtilis DesK histidine kinase(American Society for Microbiology, 2019-11-26) Fernández, Pilar; Porrini, Lucía; Albanesi, Daniela; Abriata, Luciano Andrés; Dal Peraro, Matteo; De Mendoza, Diego; Mansilla, María Cecilia