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Supernatant samples were collected by filtration, using 0.02 µm PES membrane sterile filters, after one week of growth. A fraction was collected and further treated for metabolome or proteome analysis before mineral precipitation. The rest of the sample was frozen at  20°C and afterwards thawed at room temperature (21°C) to induce struvite precipitation. Minerals were removed from the sample by sterile filtering again and the supernatant was further treated as samples after mineral precipitation. Proteins of the sterile filtered, cell-free culture supernatant were precipitated using 25% TCA (v/v). The protein pellet was washed with acetone (100%) and dried. Precipitates were resolubilized in 50 mM TEAB (triethyl ammonium bicarbonate) in 1:1 TFE:H2O (v/v). Subsequently, cysteine thiols were reduced and carbamidomethylated in one step for 30 min at 70°C by addition of each 2 µL of 500 mM TCEP (tris(2-carboxyethyl)phosphine) and 625 mM 2-chloroacetamide (CAA). The samples were further cleaned by MeOH/chloroform/H2O precipitation following the protocol of Wessel and Flügge [36].  Protein precipitates were resolubilized in 5% trifluoroethanol of aqueous 100 mM TEAB and digested overnight (18 h) with a Trypsin+LysC mixture (Promega, Walldorf, Germany) at a protein to protease ratio of 25:1. Peptides were further prepared by washing with water-saturated ethylacetate (Yeung and Stanley, [37]. Samples were evaporated to dryness in a vacuum concentrator (Eppendorf, Leipzig, Germany) and resolubilized in 30 µL of 0.05% TFA in H2O/ACN 98/2 (v/v) filtered through PES 10 kDa MWCO membrane spin filters (VWR, Darmstadt, Germany). The filtrate was transferred to HPLC vials and injected into the LC-MS/MS instrument. Each sample was measured in triplicate (3 analytical replicates of 3 biological replicates). LC-MS/MS analysis was performed on an Ultimate 3000 nano RSLC system connected to a QExactive HF mass spectrometer (both Thermo Fisher Scientific, Waltham, USA). Peptide trapping for 5 min on an Acclaim Pep Map 100 column (2 cm x 75 µm, 3 µm) at 5 µL/min was followed by separation on an analytical Acclaim Pep Map RSLC nano column (50 cm x 75 µm, 2 µm). Mobile phase gradient elution of eluent A (0.1% (v/v) formic acid in water) mixed with eluent B (0.1% (v/v) formic acid in 90/10 acetonitrile/water) was performed using the following gradient: 0 min at 4% B, 5 min at 8% B, 30 min at 12% B, 75 min at 30% B, 85 min at 50% B, 90-95 min at 96% B, 95.1-120 min at 4% B. Positively charged ions were generated at spray voltage of 2.2 kV using a stainless steel emitter attached to the Nanospray Flex Ion Source (Thermo Fisher Scientific, Waltham, USA). The quadrupole/orbitrap instrument was operated in Full MS/data-dependent MS2 Top15 mode. Precursor ions were monitored at m/z 300-1500 at a resolution of 120,000 FWHM (full width at half maximum) using a maximum injection time (ITmax) of 120 ms and an AGC (automatic gain control) target of 3e6. Precursor ions with a charge state of z=2-5 were filtered at an isolation width of m/z 1.6 amu for further HCD fragmentation at 28% normalized collision energy (NCE). MS2 ions were scanned at 15,000 FWHM (ITmax=100 ms, AGC= 2e5). Dynamic exclusion of precursor ions was set to 25. The LC-MS/MS instrument was controlled by Chromeleon 7.2, QExactive HF Tune 2.8 and Xcalibur 4.0 software."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Tandem mass spectra were searched against the Streptomyces mirabilis P16B-1 genome (GenBank accession numbers CP074102 and CP074103) using Proteome Discoverer (PD) 2.4 (Thermo Fisher Scientific, Waltham, USA) and the algorithms of Mascot 2.8 (Matrix Science, Horsham, USA), Sequest HT (version of PD2.4), MS Amanda 2.0, and MS Fragger 3.5. Two missed cleavages were allowed for the tryptic digestion. The precursor mass tolerance was set to 10 ppm and the fragment mass tolerance was set to 0.02 Da. Modifications were defined as dynamic Met oxidation, phosphorylation of Ser, Thr, and Tyr, protein N-term acetylation and/or loss of methionine, as well as static Cys carbamidomethylation. A strict false discovery rate (FDR) < 1% (peptide and protein level) and a search engine score of >30 (Mascot), > 4 (Sequest HT), >300 (MS Amanda) or >8 (MS Fragger) were required for positive protein hits. The Percolator node of PD2.5 and a reverse decoy database was used for q-value validation of spectral matches. Only rank 1 proteins and peptides of the top scored proteins were counted. Label-free protein quantification was based on the Minora algorithm of PD2.4 using the precursor abundance based on intensity and a signal-to-noise ratio >5. Imputation of missing quan values was applied by using abundance values of 75% of the lowest abundance identified per sample. Differential protein abundance was defined as a fold change of >2, ratio-adjusted p-value <0.05 (p-value/log4ratio) and at least identified in 2 of 3 replicates of the sample group with the highest abundance (prevalence filter)."],"omics_type":["Proteomics"],"labhead":["Axel A. Brakhage"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department for Molecular and Applied Microbiology, Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute Jena, Leibniz-HKI"],"species":["Streptomyces Mirabilis"],"publication":["42141328 Costa FS, Krüger T, Ueberschaar N, Kniemeyer O, Brakhage A, Kothe E. Organic Molecules are Involved in Ni-Struvite Biomineralization by Streptomyces mirabilis. Mol Biotechnol. 2026 10.1007/s12033-026-01580-3"],"submitter_mail":["thomas.krueger@leibniz-hki.de"],"submitter_affiliation":["Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute"],"submitter_country":["Germany"],"pubmed_abstract":["The Gram-positive, filamentous soil bacterium Streptomyces mirabilis P16B-1 has been shown to tolerate high environmental concentrations of Ni. The extremely high metal tolerance is partly provided through biomineralization, observed for both Mg bearing struvite and Ni-struvite where Ni ions replace Mg in the mineral lattice. The minerals showed different morphologies. This led us to assume that excreted substances may have the capacity to influence the mineral formation process that occurs at a distance to the cells. Here, we could show with metabolomics and proteomics studies that 23 metabolites as well as 18 proteins potentially co-precipitate with the minerals. Secreted secondary metabolites reduced in the supernatant after mineralization were identified as ergothioneine, diacetyllegionaminic acid, nevaltophin F, and diaminonaphthalene. The compounds phenylacetaldehyde and margaric acid also reduced after mineral precipitation did not alter mineral macromorphology. In addition, ten proteins that co-precipitated with statistical significance were predicted to be secreted. Among those, a specific nickel binding protein, NikA, was reduced in high amounts from the supernatant upon crystal formation. The potential of secreted organic molecules and proteins to bind specific surfaces of the mineral thereby redirecting crystal growth in a microbially influenced biomineralization process. Implications for biotechnological metal-struvite use are discussed."],"pubmed_title":["Organic Molecules are Involved in Ni-Struvite Biomineralization by Streptomyces mirabilis."],"pubmed_authors":["Costa Flávio Silva FS, Krüger Thomas T, Ueberschaar Nico N, Kniemeyer Olaf O, Brakhage Axel A, Kothe Erika E"],"additional_accession":[]},"is_claimable":false,"name":"Organic molecules are involved in biomineralization by Streptomyces mirabilis","description":"The Gram-positive, filamentous soil bacterium S. mirabilis P16B-1 has been shown to tolerate environmental concentrations of over 100 mM of Ni. The extremely high metal tolerance is partly provided through biomineralization observed for both Mg bearing struvite and Ni-struvite where Ni ions replace Mg in the mineral lattice. The capacity to induce mineral formation even at some distance to the cell surface indicated involvement of secreted substances in the process. Here, we could show that metabolites as well as proteins in the cell free culture natant promote mineralization. At the same time, the precipitation process if induced physically leads to some co-precipitation which might hint at first insight into nucleation. Proteomics and metabolomics were performed in sterile culture supernatant before or after precipitation of crystals was induced by freezing and thawing to obtain candidates for co-precipitated organic molecules. Three compounds could be identified to be co-precipitated with minerals formed. However, none had an impact on macro-morphology of crystals if added as pure substance. Hence, the proteome secreted by the cells was screened, and evidence for involvement of a nickel binding protein, NikA, could be obtained.","dates":{"publication":"2026-07-07","submission":"2024-02-19"},"accession":"PXD049698","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","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:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","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:1310173","NEWT:37919","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","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:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","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:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:29466","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:2003758","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","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:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","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:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:9900","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:9979","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:35231","NEWT:1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