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After approximately 16 h, when cultures reached the stationary phase, cells were transferred to fresh TY medium without antibiotics and incubated for 4 hours to reactivate cell metabolism. Once the cultures reached an OD600 of approximately 1.5 - 1.8, Erlenmeyers containing GSM pH 7.0 were inoculated with a dilution of 1/70 of the initial culture, resulting in an initial OD600 of 0.025. At the initial time (t0h without stress) there were 12 cultures of wt cells and 12 cultures of ∆actJ cells. Upon reaching an OD600 of 0.5, stress conditions were applied to each strain as follows: 4 control replicates in GSM pH 7.0, 4 replicates with GSM pH 7.0 supplemented with 185 μM of CuSO4 and 4 replicates with GSM pH 7.0 supplemented with 25 μM of ZnSO4. Cells were cultured for 2 h and aliquots were taken at t0h and t2h for viable cell counts. After 2 h of incubation, 2 ml of culture from each condition and strain were harvested. For this, 2 ml of culture were placed in 2 ml plastic tubes and centrifuged at maximum speed for 3 min at room temperature. The supernatant was discarded and the cells were washed with a solution containing 1 tablet of cOmplete Mini EDTA-free (Roche) dissolved in 10 ml of PBS. The samples were centrifuged again at maximum speed for 3 min and the supernatant was discarded. The pellets were frozen in liquid nitrogen and stored at -80 °C.  For digestion withtrifluoroethanol (TFE, Fluka), the pellets were resuspended in 100 μl of 100 mM ammonium bicarbonate prepared in Milli-Q water. Subsequently, 100 μl of TFE and 5 μl of 200 mM dithiothreitol (DTT) were added. The mixture was gently inverted to mix and incubated for 60 min in a heat block at 60 °C with shaking at 300 rpm. Then, 20 μl of 200 mM iodoacetamide was added, mixed by inversion, and incubated for 90 min at room temperature. The resulting solution was divided into two tubes, mixed with 437 μl of 100 mM ammonium bicarbonate and then with 437 μl of Milli-Q water. Finally, 10 μl of trypsin (Promega Gold) at a concentration of 1 μg/μl was added to each tube. The samples were incubated overnight at 37 °C."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["The data acquired from the Q-Exactive Plus spectrometer was processed using the Proteome Discoverer program (Thermo Scientific) and the hits were associated with the UniProt database (http://www.uniprot.org/). Data processing was carried out using Perseus 2.0.11. To determine differential proteins, a two-sample statistical analysis was performed, comparing the replicates obtained for S. meliloti 2011 wt and ΔactJ cells under different conditions: control, CuSO4 addition stress (185 μM) and ZnSO4 addition stress (25 μM). The following cut-off values were used to consider a protein as differential: p-value ≤ 0.05 and FC ≥ 2 and ≤ -2. In addition, those proteins that were found to be turned on (on, detected in all ΔactJ replicates and not detected in at least 3 of the 4 wt replicates) and off (off, not detected in at least 3 of the 4 ΔactJ replicates and detected in all wt replicates) were also determined. These proteins, whether found on or off, have no statistical value associated."],"omics_type":["Proteomics"],"labhead":["Del Papa María Florencia"],"instrument_platform":[""],"labhead_affiliation":["Instituto de Biotecnologia y Biologia Molecular. Departamento de Ciencias Biologicas, Facultad de Ciencias Exactas, Universidad Nacional de La Plata. CONICET, Argentina"],"submission_type":["PARTIAL"],"species":["Bacteria","Sinorhizobium Meliloti 2011"],"publication":["10.1111/1462-2920.70329"],"submitter_mail":["carolinavacca@biol.unlp.edu.ar"],"submitter_affiliation":["Instituto de Biotecnología y Biología Molecular, Universidad Nacional de La Plata, Argentina"],"submitter_country":["Argentina"],"additional_accession":[]},"is_claimable":false,"name":"ActJK Signal Transduction System Contributes to Copper and Zinc Resistance in Sinorhizobium meliloti","description":"Two‐component systems (TCS) play a vital role in bacterial adaptation to environmental stresses, including acid and metal toxicity. The ActJK system has been previously identified as a key regulator of acid tolerance in Sinorhizobium meliloti, a model organism for studying rhizobia‐legume symbioses. Here, we expand the functional scope of ActJK, demonstrating its involvement in responses to copper and zinc stress. Using transcriptional fusion assays, we observed the ActJK's operon activation through degP1's upstream promoter region induction by Cu2+ and Zn2+ in a dose‐dependent manner, a response absent in the ΔactJ mutant. Comparative proteomic analysis revealed distinct yet related overlapping regulatory pathways under Cu2+ and Zn2+ stress, with differentially expressed proteins suggesting convergence in efflux pump regulation and stress response mechanisms. The ΔactJ mutant displayed reduced tolerance to metal stress, impaired expression of metal detoxification genes, and altered antibiotic susceptibility profiles. Together, these findings highlight the intricate interplay between metal resistance and multidrug efflux systems in S. meliloti and underscore ActJK as a vital regulator integrating responses to environmental fluctuations. Understanding these regulatory mechanisms enhances our knowledge of bacterial survival in soil and rhizosphere under abiotic stress conditions and offers potential applications for optimising agricultural inoculants for acidic and metal‐contaminated 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