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Main cultures were then established by inoculating fresh 2 mL LB medium with a 1:1000 dilution of the overnight cultures and incubating under the same conditions for 24 h. The OD600 of each culture was adjusted to 2.5, and 2 mL of culture was washed twice with cold 1× PBS by centrifugation at 4 °C, 13,000 rpm for 3 min. Before the final centrifugation, cell counts were determined by flow cytometry using 10 µL of washed culture diluted in 990 µL of 1× PBS. Pellets were lysed with 300 µL NEBExpress E. coli Lysis Reagent (Catalog# P8116S, NEB) at room temperature for 30 min, followed by centrifugation at 16,600 × g for 10 min. A total of 250 µL of supernatant was collected for protein analysis. Protein concentration was measured using a BCA assay (Catalog# 23225, Thermo Fisher Scientific). Cell lysates diluted 5- and 10-fold were loaded (25 µL per well) into a 96-well plate, mixed with 200 µL BCA working reagent (50:1, Reagent A:B), and shaken for 30 s. Plates were incubated at 37 °C for 30 min, cooled at room temperature for 5 min in the dark, and absorbance was measured at 562 nm. Protein concentrations were calculated from a standard curve generated using protein standards. Protein analysis for both WT and mutant was conducted by the proteomics service at UT Health’s Clinical and Translational Proteomics Service Center (Houston, TX). The samples underwent acetone precipitation, during which proteins were precipitated by exposing them to –20 °C for 3 hours. Following this, a centrifugation step at 12,000 x g for 5 min separated the precipitated pellets. These pellets were subsequently subjected to denaturation and reduction using a mixture containing 30 μL of 6 M urea, 20 mM DTT in 150 mM Tris HCl (pH 8.0) at 37 °C for 40 min. Afterward, alkylation was carried out with 40 mM iodoacetamide in the absence of light for 30 min. To prepare for digestion, the reaction mixture was diluted 10-fold using 50 mM Tris-HCl (pH 8.0) and then incubated overnight at 37 °C with trypsin at a 1:30 enzyme-to-substrate ratio. The digestion process was terminated by adding an equal volume of 2% formic acid, followed by desalting using Waters Oasis HLB 1 mL reverse phase cartridges, following the vendor’s recommended procedure. Finally, the elutes were dried using vacuum centrifugation. Approximately 1 µg of the tryptic digest, prepared in a solution containing 2% acetonitrile and 0.1% formic acid in water, underwent analysis using LC/MS/MS. The instrument used was the Orbitrap Fusion Tribrid mass spectrometer by Thermo Fisher Scientific, connected to a Dionex UltiMate 3000 Binary RSLCnano System. The separation of peptides occurred on an analytical C18 column with dimensions of 100 μm ID x 25 cm, featuring 5 μm particles and an 18 Å pore size. Peptides were eluted at a flow rate of 350 nL/min. The gradient conditions applied were as follows: a gradient starting from 3% B and increasing to 22% B over a duration of 90 min, followed by a step to 22–35% B for 10 min, then another step to 35–90% B for 10 min, and finally, maintaining 90% B for an additional 10 min (Solvent A was composed of 0.1% formic acid in water, while solvent B contained 0.1% formic acid in acetonitrile). The peptides were analyzed using a data-dependent acquisition method. The Orbitrap Fusion MS operated by measuring FTMS1 spectra with a resolution of 120,000 FWHM, scanning in the m/z range of 350–1500, using an AGC target set to 2E5, and with a maximum injection time of 50ms. Within a maximum cycle time of 3 s, ITMS2 spectra were collected in rapid scan mode. High Collision Dissociation (HCD) was employed with a normalized collision energy (NCE) of 34, an isolation window of 1.6 m/z, an AGC target set to 1E4, and a maximum injection time of 35ms. Dynamic exclusion was implemented for a duration of 35 s to prevent repeated analysis of the same ions. For the experimental analysis, the Thermo Fisher Scientific Proteome Discoverer software version 1.4 was utilized to process the raw data files. The spectra were subjected to analysis against the E. coli proteome database (Swiss-Prot 29,161) through the Sequest HT search engine. Additionally, the spectra were compared against a decoy database, employing a target false discovery rate (FDR) of 1% for stringent criteria and 5% for more relaxed criteria. The enzymatic cleavage allowance for trypsin included up to two potential missed cleavages. The MS tolerance was defined as 10 ppm, while the MS/MS tolerance was set at 0.6 Da. Fixed modification involved carbamidomethylation on cysteine residues, and variable modifications encompassed methionine oxidation and asparagine deamidation."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Data processing followed the analysis steps outlined by Aguilan et al. P-value calculation was performed using a parametric t-test. The selection of the appropriate t-test type was guided by an F-test, which evaluated whether the replicates for each protein exhibited homoscedasticity (equal variances) or heteroscedasticity (unequal variances). The STRING tool (version 12.0) was used to identify significant protein–protein interaction networks among the input proteins."],"omics_type":["Proteomics"],"labhead":["Mehmet Orman"],"instrument_platform":[""],"labhead_affiliation":["Department of Biomedical Engineering, University of Wisconsin-Madison"],"species":["Escherichia Coli"],"submission_type":["PARTIAL"],"publication":["Not available"],"submitter_mail":["hgngo@wisc.edu"],"submitter_affiliation":["University of Wisconsin-Madison"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Glycerol-Driven Energy and Proteostasis Underpin Antibiotic Tolerance in Escherichia coli","description":"Bacterial persisters are frequently described as metabolically dormant, yet the endogenous metabolic programs that sustain survival during prolonged nutrient limitation remain poorly understood. Here, using stationary-phase Escherichia coli as a model of antibiotic tolerance, we combine proteomics, genetics, metabolic phenotyping, and single-cell imaging to define a metabolic framework underlying persistence. Perturbation of tricarboxylic acid cycle function broadly reprogrammed stationary-phase physiology, suppressing lipid and glycerol metabolism, altering energy homeostasis and proteostasis, and reducing antibiotic tolerance. Systems-level analyses identified phospholipid-derived glycerol catabolism as a central metabolic node linking endogenous carbon recycling to persistence. Genetic disruption of glycerol utilization impaired proton motive force homeostasis, reduced formation of large polar protein aggregates, altered division-associated remodeling, and sensitized cells to antibiotic-induced lysis. Functional metabolic assays further revealed that persisters retain a selective capacity to utilize glycerol for rapid proton motive force restoration without growth resumption. Together, our findings support a model in which stationary-phase persisters are not metabolically inert but sustained through endogenous metabolic rewiring that coordinates energy maintenance, proteostasis, and antibiotic 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