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Supernatant and pellet were separated and extracellular/secreted proteins in the supernatant were precipitated by adding 1 mL cold 80 % trichloroacetic acid (TCA), incubated over night at 4 ˚C, and centrifuged at 4,500 × g for 30 minutes. The protein pellet was washed with 90 % acetone in 0.01M HCl, recentrifuged, supernatant discarded, and the pellet was air dried. For extraction of intracellular proteins, 500 µL lysis buffer (4 % SDS in H2O) was added to the initial cell pellet and kept on ice for 30 min, followed by mechanical cell disruption by beat-beating with FastPrep24 (Thermo Fisher Scientific) and glass beads (particle size ≤ 106 μm; Sigma) for three cycles of 60 sec at 4.5 m/s. The samples were then centrifuged for 15 min at 15,000 × g at 4 °C and the supernatant containing soluble intracellular proteins were used to redissolve the pellet containing extracellular proteins above. These rejoined samples were then reduced, alkylated, and digested with trypsin following the S-Trap 96-well plate digestion protocol (ProtiFi, USA) according to the manufacturer’s instructions. Peptides were eluted from the plates in 40 % acetonitrile, dried in a speed vac and redissolved in 0.1% formic acid prior to LC-MS analysis. Peptides were analyzed by nanoLC-MS/MS using a Dionex Ultimate 3000 HPLC (Dionex, Sunnyvale CA, USA) connected to a Q-Exactive hybrid quadrupole-orbitrap mass spectrometer (Thermo Fisher, Bremen, Germany) equipped with a nano-electrospray ion source. The peptides were loaded onto a trap column (Acclaim PepMap 100, C18, 5 µm, 100 Å, 300 µm i.d. × 5 mm, Thermo Scientific, Bremen, Germany) and backflushed onto an analytical column (Acclaim PepMap RCLS, C18, 3 µm, 100 Å, 75 µm i.d. × 50 cm, Thermo Scientific, Bremen, Germany). The flow rate was 300 nL/min and the solvent gradient was 3-35 % B in 65 min, to 60 % B in 3 min, and followed by a further increase to 80 % B for column washing. Solvent A was 0.1 % (v/v) formic acid and solvent B was 100 % (v/v) acetonitrile, 0.1 % (v/v) formic acid. The Q-Exactive mass spectrometer was operated in data-dependent mode acquiring one full scan (400-1500 m/z) at R=70,000 followed by (up to) 12 dependent MS/MS scans at R=35,000."],"repository":["pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Protein identification and quantification was performed using Fragpipe v20.0 using the workflow LFQ-MBR. The predicted protein-coding genes from the metagenomic analysis were used as reference database (5,057,886 protein sequences). This large database necessitated utilizing a high-end Linux computer and without software calibration of m/z-values in the instrument RAW files; however, the mass spectrometer was externally calibrated prior to the analysis and yielded an accuracy of ~5 ppm. In addition, reversed sequences of all protein entries were concatenated to the database for estimation of false discovery rates. The tolerance level for matching to the database was 20 ppm for both MS and MS/MS. N-terminal acetylation and methionine oxidation were set as variable modifications while carbamidomethylation of cysteines were set as fixed modifications. Trypsin was used as digestion enzyme and one missed cleavage was allowed. Quantification was done using the LFQ Top N (n=3) algorithm, and the feature ‘Match between runs’ was applied with an FDR of 1%. Further, all final identifications were filtered to 1% FDR in Fragpipe using ProteinProphet, and identifications of potential contaminants and reversed sequences were removed. Proteins were considered identified if present in two of three replicate enrichment samples for at least one lake. Metagenomic annotations (taxonomy, MAG) as well as functional annotations from KoFam, and dbCAN databases were propagated to the metaproteomics data. To calculate protein abundances per MAG, protein hits containing indistinguishable proteins originating from other species were omitted to limit noise from cross-species protein-groups contamination. LFQ values were then summed per MAG."],"omics_type":["Proteomics"],"labhead":["Magnus Øverlie Arntzen"],"instrument_platform":[""],"labhead_affiliation":["Norwegian University of Life Sciences"],"submission_type":["PARTIAL"],"species":["Bacteria"],"publication":["Not available"],"submitter_mail":["magnus.arntzen@nmbu.no"],"submitter_affiliation":["Norwegian University of Life Sciences"],"submitter_country":["Norway"],"additional_accession":[]},"is_claimable":false,"name":"Microbial consortia mediating lignocellulose turnover and denitrification in eutrophic lake sediment enrichments","description":"Anthropogenic activities such as urbanization and agriculture can potentially pose a threat to neighboring freshwaters through nitrate and phosphorous contamination, which over time may lead to lake eutrophication. In such nitrogen-polluted environments, oxygen is depleted, and plants die and decompose. This enhances denitrifying microbes that respire under hypoxic/anoxic conditions by reducing nitrate instead of molecular oxygen and using plant remnants (lignocellulose) as carbon source. Microbial lignocellulose degradation has been well-studied for both aerobic- and anaerobic conditions; however, its degradation during denitrification remains largely unknown. Here we have applied a combination of gas kinetics and meta-omics techniques to enrich and analyze microbial communities from 10 eutrophic lakes to identify a set of core microbial metagenome-assembled genomes (MAGs) present in all the eutrophic lakes. We have further investigated their strategies and enzyme profiles for degrading lignocellulose under denitrifying conditions. We identified Pseudomonadota, Bacteroidota, Verrucomicrobiota, and Actinomycetota as the most abundant phyla and they were present in enrichments from all eutrophic lakes having a key role in denitrification and fermentation. Lignocellulose degradation was, however, dominated by species outside the core microbiome, i.e., there were differing key degraders between lakes, suggesting some level of lake-specialization. Among these we observed potential respiratory DNRA pathways, and they expressed a broad range of CAZymes targeting the various lignocellulose subfractions. Interestingly, many of the detected MAGs contained NO dismutases, enzymes postulated to convert NO to molecular oxygen and dinitrogen 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