{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/r2.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/r1.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/w3.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/LutR_LFQ_submit.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/w2.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/r3.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/w1.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/zsp-R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/zsp-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/zsp-w2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/zsp-w1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/zsp-R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/zsp-w3.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/w2.ssl","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/r1.sepr","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/w2.sepr","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/r3.ssl","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/r2.sepr","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/r3.sepr","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/r2.ssl","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/w3.sepr","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/w3.ssl","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/r1.ssl","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/w11.ssl","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/01/PXD008578/w1.sepr"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["zhangmy16@lzu.edu.cn"],"submitter":["Meng-Yuan Zhang"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"disease":["Wounds And Injuries"],"software":[""],"submitter_keywords":["Pseudomonas fluorescens lc-msms proteomics"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD008578"],"tissue":["Sperm","Whole Body"],"sample_protocol":["The bacterial suspension was inoculated into two flasks and induced with indole of 1 mM and equal volume of DMSO for 8 hours, respectively. Cells were collected by spinning at 6000 g and washed twice with PBS. The pellet was resuspended and lysised with 200 mL lysis buffer at 100℃ for 10 minutes. Then the chromatin was sheared by sonicating for 30 minutes at room temperature. The appropriate volume of dilution buffer was added to dilute the urea to a final concentration of 800 uM . Trypsin digestion was typically employed at 37℃ overnight."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The raw mass spectrometry files were analyzed by patternlab 4.0.  MS/ MS spectra were searched  against 2p24 fasta database choosing carboxymethyl (C), and oxidation (M) as variable modifications and allowing enzyme specificity at one terminus only. Peptide and fragment tolerances were set at 10 ppm and xxmmu, respectively. Finally , we identified ~1700 proteins   张四萍 1/2/2018 9:40:35 下午 The extraction of total protein and Mass spectrometry The bacterial cells of WT and ΔAgtR in the stationary phase were collected, lysed, reducted and alkylated according to modified protocol of Matthias Mann et al(37)（ref）. The peptides samples were normalized with BCA kit before loading onto MS analyzer.`` The peptides were analyzed on a nanoflow UPLC system coupled online by a nanospray ion source  to an Orbitrap fusion lumos  mass spectrometer (Thermo-Fisher Scientific). The peptides were separated on two successive reverse phase columns using a linear gradient (xx-xx% acetonitrile in 90 min) and a constant flow rate of 300 nL/min. Fragmentation was performed using higher energycollision induced dissociation (HCD) and sequenced precur-sor ions were dynamically excluded for xxsec. The raw mass spectrometry files were analyzed by patternlab 4.0.  MS/ MS spectra were searched  against 2p24 fasta database choosing carboxymethyl (C), and oxidation (M) as variable modifications and allowing enzyme specificity at one terminus only. Peptide and fragment tolerances were set at 10 ppm"],"omics_type":["Proteomics"],"labhead":["Zhang-Meng Yuan"],"instrument_platform":[""],"labhead_affiliation":["LanZhou University"],"submission_type":["PARTIAL"],"species":["Pseudomonas Fluorescens F113"],"submitter_mail":["zhangmy16@lzu.edu.cn"],"publication":["30680880 Wang Y, Zhang SP, Zhang MY, Kempher ML, Guo DD, Han JT, Tao X, Wu Y, Zhang LQ, He YX. The antitoxin MqsA homolog in Pseudomonas fluorescens 2P24 has a rewired regulatory circuit through evolution. Environ Microbiol. 2019 10.1111/1462-2920.14538"],"curator_keywords":["Biological"],"submitter_affiliation":["Lanzhou University"],"submitter_country":["China"],"pubmed_abstract":["The mqsRA operon encodes a toxin-antitoxin pair that was characterized to participate in biofilm and persister cell formation in Escherichia coli. Notably, the antitoxin MqsA possesses a C-terminal DNA-binding domain that recognizes the [5'-AACCT(N)<sub>2-4</sub> AGGTT-3'] motif and acts as a transcriptional regulator controlling multiple genes including the general stress response regulator RpoS. However, it is unknown how the transcriptional circuits of MqsA homologues have changed in bacteria over evolutionary time. Here, we found mqsA in Pseudomonas fluorescens (PfmqsA) is acquired through horizontal gene transfer and binds to a slightly different motif [5'-TACCCT(N)<sub>3</sub> AGGGTA-3'], which exists upstream of the PfmqsRA operon. Interestingly, an adjacent GntR-type transcriptional regulator, which was termed AgtR, is under negative control of PfMqsA. It was further demonstrated that PfMqsA reduces production of biofilm components through AgtR, which directly regulates the pga and fap operons involved in the synthesis of extracellular polymeric substances. Moreover, through quantitative proteomics analysis, we showed AgtR is a highly pleiotropic regulator that influences up to 252 genes related to diverse processes including chemotaxis, oxidative phosphorylation and carbon and nitrogen metabolism. Taken together, our findings suggest the rewired regulatory circuit of PfMqsA influences diverse physiological aspects of P. fluorescens 2P24 via the newly characterized AgtR."],"pubmed_title":["The antitoxin MqsA homologue in Pseudomonas fluorescens 2P24 has a rewired regulatory circuit through evolution."],"pubmed_authors":["Wang Yong Y, Zhang Si-Ping SP, Zhang Meng-Yuan MY, Kempher Megan L ML, Guo Ding-Ding DD, Han Jian-Ting JT, Tao Xuanyu X, Wu Yi Y, Zhang Li-Qun LQ, He Yong-Xing YX"],"additional_accession":[]},"is_claimable":false,"name":"pseudomonas fluorescens LC-MSMS","description":"our work revealed a rewired regulatory network of mqsA in P. fluoresces, in which a new transcription factor is recruited and incorporated to fulfill the similar physiological 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