{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/Woo_et_al_Proteomics.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/LSM1_HSM-R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/JE3692_HSM-R4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/JE3692_HSM-R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/LSM1_HSM-R4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/JE3692_Glc-R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/LSM1_Glc-R4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/JE3692_Glc-R4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/JE3692_HSM-R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/LSM1_HSM-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/LSM1_Glc-R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/LSM1_HSM-R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/JE3692_HSM-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/LSM1_Glc-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/JE3692_Glc-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/JE3692_Glc-R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD055215/LSM1_Glc-R2.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["cjpetzold@lbl.gov"],"submitter":["Christopher Petzold"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Lignocellulose","Adaptive laboratory evolution (ale)","Proteomics","Pseudomonas putida"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD055215"],"sample_protocol":["Protein was extracted from cell pellets and tryptic peptides were prepared by following established proteomic sample preparation protocol. Briefly, cell pellets were resuspended in Qiagen P2 Lysis Buffer (Qiagen, Germany) to promote cell lysis. Proteins were precipitated with addition of 1 mM NaCl and 4 x vol acetone, followed by two additional washes with 80% acetone in water. The recovered protein pellet was homogenized by pipetting mixing with 100 mM ammonium bicarbonate in 20% methanol. Protein concentration was determined by the DC protein assay (BioRad, USA). Protein reduction was accomplished using 5 mM tris 2-(carboxyethyl)phosphine (TCEP) for 30 min at room temperature, and alkylation was performed with 10 mM iodoacetamide (IAM; final concentration) for 30 min at room temperature in the dark. Overnight digestion with trypsin was accomplished with a 1:50 trypsin:total protein ratio."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["DIA raw data files were analyzed by an integrated software suite DIA-NN. The databases used in the DIA-NN search (library-free mode) are P. putida KT2440 latest Uniprot proteome FASTA sequences plus the protein sequences of the heterologous proteins and common proteomic contaminants. DIA-NN determines mass tolerances automatically based on first pass analysis of the samples with automated determination of optimal mass accuracies. The retention time extraction window was determined individually for all MS runs analyzed via the automated optimization procedure implemented in DIA-NN. Protein inference was enabled, and the quantification strategy was set to Robust LC = High Accuracy. Output main DIA-NN reports were filtered with a global FDR = 0.01 on both the precursor level and protein group level. The Top3 method, which is the average MS signal response of the three most intense tryptic peptides of each identified protein, was used to plot the quantity of the targeted proteins in the samples."],"omics_type":["Proteomics"],"labhead":["Christopher J. Petzold"],"instrument_platform":[""],"labhead_affiliation":["Staff Scientist Biological Systems & Engineering Division Lawrence Berkeley National Laboratory Berkeley CA 94720"],"submission_type":["PARTIAL"],"species":["Pseudomonas Putida Kt2440"],"submitter_mail":["cjpetzold@lbl.gov"],"publication":["Not available"],"submitter_affiliation":["Lawrence Berkeley National Laboratory"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Simultaneous Optimization of Multi-lignocellulosic-sugar Catabolism via Systematic Laboratory Evolution in Dynamic Conditions","description":"The development of microbial bioproduction is challenged by the complexity and variability of industrial feedstocks. This study aimed to systematically and simultaneously optimize catabolism of multiple sugars present in common renewable lignocellulose by adaptive laboratory evolution (ALE) using dynamic selection regimes. The engineered strain, JE3692, was subjected to ALE using three dynamic regimes— a high sugar mixture (HSM), low sugar mixture (LSM), and glucose-xylose-arabinose (GXA) series—and was compared with static ALE protocols using individual sugars. Physiological characterization of evolved strains revealed that the LSM strategy yielded the most significant improvements in catabolic efficiency and growth rates under industrially relevant mixed sugar conditions. Genomic analysis identified key mutations in heterologous pathways that contributed to the enhanced catabolism of xylose and arabinose, while proteomic analysis linked these mutations to changes in protein expression profiles in the LSM1 strain. The LSM1 strain demonstrated superior performance in producing the value-added product indigoidine, highlighting the potential of dynamic ALE for developing robust microbial strains for industrial bioproduction using lignocellulosic 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