D
Diego de Mendoza
Researcher at National University of Rosario
Publications - 138
Citations - 6267
Diego de Mendoza is an academic researcher from National University of Rosario. The author has contributed to research in topics: Bacillus subtilis & Membrane fluidity. The author has an hindex of 45, co-authored 129 publications receiving 5753 citations. Previous affiliations of Diego de Mendoza include University of Illinois at Urbana–Champaign & National Scientific and Technical Research Council.
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Journal ArticleDOI
Molecular basis of thermosensing: a two-component signal transduction thermometer in Bacillus subtilis.
Pablo S. Aguilar,Ana M. Hernández-Arriaga,Larisa E. Cybulski,Agustín C. Erazo,Diego de Mendoza +4 more
TL;DR: A regulatory loop composed of a sensor kinase, DesK, and a response regulator, DesR, responsible for cold induction of the des gene coding for the Δ5‐lipid desaturase from Bacillus subtilis provides a novel mechanism for the control of gene expression at low temperatures.
Journal ArticleDOI
Control of Membrane Lipid Fluidity by Molecular Thermosensors
TL;DR: Bacteria can encounter a wide range of environments and must adapt to new conditions in order to survive and the barrier function of the cytoplasmic membrane is known to depend on the plasma membrane.
Journal ArticleDOI
A Bacillus subtilis Gene Induced by Cold Shock Encodes a Membrane Phospholipid Desaturase
TL;DR: This is the first report of a membrane phospholipid desaturase in a nonphotosynthetic organism and the first direct evidence for cold induction of a desaturases.
Journal ArticleDOI
Thermal regulation of membrane lipid fluidity in bacteria
Diego de Mendoza,John E. Cronan +1 more
TL;DR: Bacteria regulate the fluidity of their membrane phospholipids in response to temperature through the activity of a soluble enzyme, β-ketoacyl-acyl carrier protein synthase II, of the fatty acid biosynthetic pathway.
Journal ArticleDOI
Structural plasticity and catalysis regulation of a thermosensor histidine kinase
Daniela Albanesi,Mariana Martín,Felipe Trajtenberg,María C. Mansilla,Ahmed Haouz,Pedro M. Alzari,Diego de Mendoza,Alejandro Buschiazzo +7 more
TL;DR: It is shown that the thermosensitive histidine kinase, DesK, from Bacillus subtilis is cold-activated through specific interhelical rearrangements in its central four-helix bundle domain, suggesting a model in which the transmembrane sensor domain of DesK promotes these structural changes through conformational signals transmitted by the membrane-connecting two-helical coiled-coil.