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Four-day-old seedlings were inoculated by pipetting 1 ml of bacterial inoculum (OD600 = 0.01) or PBS (mock) along the root tips and further grown vertically in the tissue culture room. At 12, 24, and 36 hpi, roots were cut and snap-frozen in liquid nitrogen. Plant material was harvested in four biological replicates. The finely ground Arabidopsis root material was homogenized in 5 mL extraction buffer [50 mM Tris-HCl (pH 8), 30% (w/v) sucrose, 0.1 M KCl, 5 mM EDTA, and 1 mM dithiothreitol (DTT) (Sigma-Aldrich) in Milli-Q water containing appropriate amounts of cOmplete™ ULTRA tablets EDTA-free (Roche) and PhosSTOP (Roche)]. Samples were sonicated for 30 s (2 s on and 2 s off) followed by a centrifugation step at 4 ⁰C for 15 min at 3166 g. Supernatant was collected and 15 mL methanol, 5 mL chloroform, and 20 mL H2O was added. Samples were shaken vigorously and centrifuged for 15 min at room temperature at 3166 g. The upper aqueous phase was removed and 20 mL methanol was added, and after mixing, samples were centrifuged for 15 min at room temperature at 3166 g. The supernatant was discarded and the pellet was washed using 5 mL 80% acetone. Next, samples were centrifuged for 10 min at room temperature at 3166 g, after which the supernatant was discarded and samples were air dried. The protein pellets were solubilized in 0.25 mL 8 M urea in 50 mM triethylammonium bicarbonate buffer. Freshly prepared 750 mM tris(2-carboxyethyl)phosphine-HCl (TCEP, pH 8) and 750 mM iodoacetamide were added to a final concentration of 15 mM and 30 mM, respectively. The samples were shaken at 30 ⁰C in the dark for 15 min, followed by centrifugation for 5 min at room temperature at 3166 g. The total protein amount in the supernatant was quantified with a Nanodrop and 2.5 mg protein material was pre-digested with 10 μg EndoLysC (1:250 ratio, Wako) at 37 ⁰C with mixing for 2 h. The samples were diluted 8 times with 50 mM tetraethylammonium bromide (TEAB) and 10 μg trypsin (Promega) was added per mg sample (1:100 ratio). The samples were kept at 37 ⁰C overnight while shaking. To stop the digestion, trifluoroacetic acid (TFA) was added to obtain a pH ≤ 3. The samples were desalted with C18 ODS columns (Agilent) and then dried in a SpeedVac vacuum concentrator. The dried eluates were resuspended in 500 μL of loading buffer (80% acetonitrile, 6% TFA) and incubated with 1 mg of MagReSyn Ti-IMAC microspheres (ReSyn Biosciences) for 20 min at room temperature while mixing. The supernatant was removed and another 500 μL of loading buffer was added for 30 s to remove unbound samples. Next, the microspheres were washed once with 500 μL wash buffer A (60% acetonitrile, 1% TFA, 200 mM NaCl) for 2 min and twice with 500 μL wash buffer B (60% acetonitrile, 1% TFA) with gentle agitation. The bound phosphopeptides were eluted by adding 80 μL elution buffer (40% ACN, 1% NH4OH) in 15 min while mixing. Next, 6 μL of 100% formic acid was added to the first 80 μL eluate to acidify the solution. This elution was repeated twice to reach a final elution volume of 240 μL. The 3 eluates were collected into a mass spec vial, vacuum dried and analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) as previously described."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["MS/MS spectra were searched against the TAIR11 database for Arabidopsis (version June 2016) by the MaxQuant software (version 1.6.11.0). Carbamidomethylation of Cys residues was set as fixed modification, whereas Met oxidation, protein N-terminal acetylation and Ser/Thr/Tyr phosphorylation were set as variable modifications. MaxQuant settings are listed in Table S1. The ‘Phospho(STY).txt’ output file generated by the MaxQuant search was loaded into the Perseus software (version 1.6.10.50) for analysis. All the data were selected first by a phosphorylation localization probability cut-off of > 0.75. Log2-transformed phosphopeptide intensities were used for further analysis. Of the 22,689 phosphopeptides identified and quantified in total, 7,068 phosphopeptides were retained for evaluation after filtering phosphopeptides with at least three valid values in at least one treatment group. To account for missing values, we applied a hybrid approach, in which both peptide intensities and their presence or absence under certain conditions or at certain time points were considered. Hence, to determine one final RHG1 and one final Bacillus specific response, we carried out two separate analyses. First, we detected phosphopeptides that were present or absent in a certain bacterial treatment, for each time point separately. For the identification of phosphopeptides under RHG1 conditions, we screened their occurrence in a minimum of three out of four repeats and absence or discovery only once in each of the control conditions, i.e., mock and Bacillus. To identify phosphopeptides absent under RHG1 conditions, we screened for those either not detected or detected only once, while being consistently present (in at least three out of four replicates) in both control conditions, i.e., mock and Bacillus. In a similar way, we selected phosphopeptides present or absent under Bacillus conditions, by means of mock- and RHG1-treated samples as control conditions. The other intensity-based analysis consisted of the detection of phosphopeptides, separately for each time point, with a significant (P < 0.05) differential abundance pattern when two treatments were compared and in three comparisons: RHG1 versus mock, Bacillus versus mock, and RHG1 versus Bacillus. The three resulting phosphopeptide lists were further separated in enriched and depleted phosphopeptides. To identify the RHG1- or Bacillus-specific phosphopeptide response, we selected for each time point separately, the phosphopeptides present in both the RHG1 versus mock and RHG1 versus Bacillus list, or the Bacillus versus mock and the Bacillus versus RHG1 list, respectively. Heatmaps were created by substituting the missing values with the lowest detected value in the entire dataset, after which the average value over the four biological replicates was calculated for each phosphopeptide of interest. In Perseus (version 1.6.14.0), the average phosphopeptide abundance values were transformed into Z-scores and rows were clustered according to standard parameters."],"omics_type":["Proteomics"],"labhead":["Sofie Goormachtig"],"instrument_platform":[""],"labhead_affiliation":["VIB-UGent Center for Plant Systems Biology, Belgium"],"submission_type":["PARTIAL"],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"submitter_mail":["shaoli.yang@ugent.be"],"publication":["Not available"],"submitter_affiliation":["VIB-UGent Center for Plant Systems Biology"],"submitter_country":["Belgium"],"additional_accession":[]},"is_claimable":false,"name":"A combined omics approach to elucidate the molecular interplay behind a beneficial Arabidopsis-Caulobacter interaction","description":"Plants rely on complex signaling networks to regulate growth and to interact with their environment, including beneficial microbes such as plant growth–promoting rhizobacteria (PGPR). Among these microbes, Caulobacter RHG1 has been shown to enhance plant growth and is recognized by Arabidopsis roots via specific receptor-like kinases (RLKs), but the molecular mechanisms underlying the plant growth-promotion effect remain largely unknown. To investigate these mechanisms, we used an integrative approach combining proteomics and phosphoproteomics to explore how RHG1 stimulates growth in Arabidopsis thaliana. Our phosphoproteome analysis revealed that RHG1 triggers a range of signaling events in the root, involving two RLKs (LysM RLK1-INTERACTING KINASE 1 [LIK1] and an uncharacterized RLK, AT5G49770). Notably, via the proteome analysis, we revealed that upon RHG1 treatment, defense proteins are downregulated early. Later on, developmental processes, such as those related to ribosome biogenesis and maturation, are involved in the growth-promotion effect and might lead to enhanced cell division and/or activity. These findings suggest that RHG1 is perceived at the root-level and this, via phosphorylation-based signaling pathways, triggers early protein-based effects that are characterized by timely modulation of defense and developmental processes, which eventually lead to plant growth promotion. Our data, combined with that of previous reports, points to the involvement of multiple signaling pathways, suggesting that RHG1 activates a broad network of regulatory mechanisms that extend beyond a single pathway. Understanding the mechanisms behind such beneficial plant-microbe interactions can pave the way for more effective commercialization of PGPR-based agricultural products, and our approach offers valuable insights for future research in this field.","dates":{"publication":"2026-04-14","submission":"2025-08-06"},"accession":"PXD066978","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2042546","NEWT:148942","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:460523","NEWT:2423","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:476","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:941638","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:300641","NEWT:39655","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:6039","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:280406","NEWT:83906","NEWT:99488","NEWT:99487","NEWT:1134506","NEWT:255470","NEWT:762903","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:266940","NEWT:287889","NEWT:9938","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:483179","NEWT:315750","NEWT:99490","NEWT:632957","NEWT:265619","NEWT:11294","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:1479235","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:105812","NEWT:11298","NEWT:4233","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:487521","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","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