(FBIOyF) Departamento de Microbiología
URI permanente para esta comunidad
Examinar
Examinando (FBIOyF) Departamento de Microbiología por Autor "Albanesi, Daniela"
Mostrando 1 - 6 de 6
Resultados por página
Opciones de ordenación
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 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