%0 Journal Article %T Multiple detection of both attractants and repellents by the dCache ‐chemoreceptor SO_1056 of Shewanella oneidensis %+ Bioénergétique et Ingénierie des Protéines (BIP ) %+ Università di Corsica Pasquale Paoli [Université de Corse Pascal Paoli] %+ Laboratoire de chimie bactérienne (LCB) %A Boyeldieu, Anne %A Poli, Jean‐pierre %A Ali Chaouche, Amine %A Fierobe, Henri‐pierre %A Giudici-Orticoni, Marie‐thérèse %A Méjean, Vincent %A Jourlin‐castelli, Cécile %< avec comité de lecture %@ 1742-464X %J FEBS Journal %I Wiley %8 2022 %D 2022 %R 10.1111/febs.16548 %K bacterial chemotaxis %K chemoreceptors %K dCache domain %K isothermal titration calorimetry %K ligand binding %K thermal shift assay %Z Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyJournal articles %X Chemoreceptors are usually transmembrane proteins dedicated to the detection of compound gradients or signals in the surroundings of a bacterium. After detection, they modulate the activation of CheA-CheY, the core of the chemotactic pathway, to allow cells to move upwards or downwards depending on whether the signal is an attractant or a repellent, respectively. Environmental bacteria such as Shewanella oneidensis harbour dozens of chemoreceptors or MCPs (methyl-accepting chemotaxis proteins). A recent study revealed that MCP SO_1056 of S. oneidensis binds chromate. Here, we show that this MCP also detects an additional attractant (L-malate) and two repellents (nickel and cobalt). The experiments were performed in vivo by the agarose-in-plug technique after overproducing MCP SO_1056 and in vitro, when possible, by submitting the purified ligand-binding domain (LBD) of SO_1056 to a thermal shift assay (TSA) coupled to isothermal titration calorimetry (ITC). ITC assays revealed a K D of 3.4 lM for L-malate and of 47.7 lM for nickel. We conclude that MCP SO_1056 binds attractants and repellents of unrelated composition. The LBD of SO_1056 belongs to the double Cache_1 family and is highly homologous to PctA, a chemoreceptor from Pseudomonas aeruginosa that detects several amino acids. Therefore, LBDs of the same family can bind diverse compounds, confirming that experimental approaches are required to define accurate LBD-binding molecules or signals. %G English %2 https://cnrs.hal.science/hal-03740302/document %2 https://cnrs.hal.science/hal-03740302/file/The%20FEBS%20Journal%20-%202022%20-%20Boyeldieu%20-%20Multiple%20detection%20of%20both%20attractants%20and%20repellents%20by%20the%20dCache_E2_80_90chemoreceptor%20SO-1.pdf %L hal-03740302 %U https://cnrs.hal.science/hal-03740302 %~ CNRS %~ UNIV-AMU