{"database":"JPOST Repository","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Wiff":["https://storage.jpostdb.org/JPST001558/files/MGM100dlon_Glc_S3.wiff.scan","https://storage.jpostdb.org/JPST001558/files/MGM100_Glc_S3.wiff.scan","https://storage.jpostdb.org/JPST001558/files/MGM100dlon_Ara_S3.wiff","https://storage.jpostdb.org/JPST001558/files/MGM100_Ara_S1.wiff.scan","https://storage.jpostdb.org/JPST001558/files/MGM100dlon_Glc_S3.wiff","https://storage.jpostdb.org/JPST001558/files/MG1655_Ara_S1.wiff.scan","https://storage.jpostdb.org/JPST001558/files/MGM100dlon_Glc_S2.wiff","https://storage.jpostdb.org/JPST001558/files/MG1655_Glc_S3.wiff.scan","https://storage.jpostdb.org/JPST001558/files/MGM100dlon_Ara_S3.wiff.scan","https://storage.jpostdb.org/JPST001558/files/MG1655_Glc_S1.wiff","https://storage.jpostdb.org/JPST001558/files/MG1655_Ara_S1.wiff","https://storage.jpostdb.org/JPST001558/files/MG1655_Glc_S1.wiff.scan","https://storage.jpostdb.org/JPST001558/files/MGM100_Ara_S3.wiff","https://storage.jpostdb.org/JPST001558/files/MGM100_Ara_S1.wiff","https://storage.jpostdb.org/JPST001558/files/MG1655_Ara_S3.wiff.scan","https://storage.jpostdb.org/JPST001558/files/MG1655_Glc_S3.wiff","https://storage.jpostdb.org/JPST001558/files/MGM100dlon_Glc_S2.wiff.scan","https://storage.jpostdb.org/JPST001558/files/MG1655_Ara_S3.wiff","https://storage.jpostdb.org/JPST001558/files/MGM100_Glc_S3.wiff","https://storage.jpostdb.org/JPST001558/files/MGM100_Ara_S3.wiff.scan"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Hideki Taguchi"],"species":["Escherichia Coli"],"full_dataset_link":["https://repository.jpostdb.org/entry/JPST001558"],"submitter_affiliation":["Tokyo Institute of Technology"],"sample_protocol":[""],"repository":["jPOST"],"data_protocol":[""],"pubmed_abstract":["The <i>Escherichia coli</i> chaperonin GroEL/ES (GroE) is one of the most extensively studied molecular chaperones. So far, ~80 proteins in <i>E. coli</i> are identified as GroE substrates that obligately require GroE for folding in vivo. In GroE-depleted cells, these substrates, when overexpressed, tend to form aggregates, whereas the GroE substrates expressed at low or endogenous levels are degraded, probably due to misfolded states. However, the protease(s) involved in the degradation process has not been identified. We conducted a mass-spectrometry-based proteomics approach to investigate the effects of three ATP-dependent proteases, Lon, ClpXP, and HslUV, on the <i>E. coli</i> proteomes under GroE-depleted conditions. A label-free quantitative proteomic method revealed that Lon protease is the dominant protease that degrades the obligate GroE substrates in the GroE-depleted cells. The deletion of DnaK/DnaJ, the other major <i>E. coli</i> chaperones, in the ∆<i>lon</i> strain did not cause major alterations in the expression or folding of the obligate GroE substrates, supporting the idea that the folding of these substrates is predominantly dependent on GroE."],"pubmed_title":["Shotgun Proteomics Revealed Preferential Degradation of Misfolded In Vivo Obligate GroE Substrates by Lon Protease in <i>Escherichia coli</i>."],"pubmed_authors":["Niwa Tatsuya T, Chadani Yuhei Y, Taguchi Hideki H"],"name_synonyms":["biochemical pathways, Alkalescens-Dispar Group, cellular breakdown, Diffusely Adherent Escherichia coli, Bacterium coli, Escherichia/Shigella coli, biodegradation, Enteroinvasive E. coli, degradation, Peptidomics, breakdown of chemical, catabolism, bacterium E3, E coli, EAggEC, Enteroaggregative E. coli, E. coli., cellular catabolism, Eschericia coli, Enteroaggregative Escherichia coli, breakdown of substance, Bacterium coli commune, Lon Protease, Diffusely Adherent E. coli, Bacillus coli, Escherchia coli, cellular degradation, biotransformation, secretion, Enteroinvasive Escherichia coli, Enterococcus coli, breakdown of molecule, Endopeptidase La"],"pubmed_abstract_synonyms":["biochemical pathways, LIP6, Forms, HSP60, l(2)tumorous imaginal discs, DNAJ, DnaJ, bacterium E3, dnaj, Chaperonin Protein Complex, DmelCG6383, Techniques, Chaperone, DmelCG8798, Method, CPN60, cellular degradation, Strain., Proteases, Enterococcus coli, Analysis, HSP65, ATP-Dependent Protease, WMS, 2010206B19Rik, me75, Escherichia/Shigella coli, Molecular, catabolism, crumb, Adenosine Triphosphate-Dependent Proteolytic System, E coli, HLD4, COXA_DROME, D17Mit170, free, ecotype, T1, E. coli, cDNA 10D, Eschericia coli, Enteroaggregative Escherichia coli, hld4, GROEL, 5730551F12Rik, Methodological Studies, MSJ-1, DJ3, dj3, DJ4, biotransformation, Strains, GPHYSD2, SGS, Endopeptidase La, 1500017M13Rik, anatomical protrusion, l(2)tud, CG6383, tid, rdj2, CG8798, Procedure, HSJ-2, Tl3, Enteroaggregative E. coli, Tl2, ACMICD, Spectroscopy, DLag1, DLAG1, Prss15, LONP, PRSS15, Diffusely Adherent E. coli, secretion, cultivar, l(2)td, Diffusely Adherent Escherichia coli, Enteroinvasive E. coli, Va, ATP-Dependent, Spectrometry, Dlag1, MASS, Methodological, dja2, 1200017E13Rik, Lag1, Methodological Study, Chaperonin Family, l(1)G0365, spine, label, lag1, l(1)G0489, mDj3, DmelCG14724, Adenosine Triphosphate Dependent Proteolytic System, CG15898, Strains and Sprains, l(3)S050920, Proteomes, RDJ2, Chaperonin, Crbs, cpr3, HDJ3, Procedures, Peptidomics, HuCHA60, number, FBN, DNJ3, l(2)701, Gene, Protease, LonHS, far, PIM1, presence, cellular catabolism, ATP phosphohydrolase (polypeptide-unfolding), PRO3015, protrusion, method, Crumbs, Lon, LON, ECTOL1, chaperonin ATPase activity, Escherchia coli, method used in an experiment, ATP Dependent Protease, Gene Products, Studies, non-chaperonin molecular chaperone ATPase activity, Enteroinvasive Escherichia coli, Low, DJA2, Sprains, Technique, dnj3, CT19912, MRJ, 0509/20, lon, breakdown of chemical, nucleoplasmin ATPase activity, peroxisome-assembly ATPase activity, Complex, Spectrum, 1384/04, CPR3, HSJ2, CG5504, OCTD, Study, ATP-Requiring Protease, hsj2, dnajb6, groel, COX, Chaperonin Complex, CG3576, HSP-60, HHDJ1, anon-WO0118547.350, DRIP78, l(3)j1B5, Alkalescens-Dispar Group, cellular breakdown, ATP-Requiring, Bacterium coli, cou, degradation, Chaperones, Proteins, Sprain, TID56, EAggEC, Molecular Chaperone, SPG13, Cell, l(3)07207, strain, count in organism, Lr, Lon Protease, Bacillus coli, hsp65, Protein, Dnaj3, CRB, Crb, MFS1, l(3)S058104, LGMD1D, l(1)G0061, LGMD1E, cpn60, WMS2, breakdown of molecule, l(2)tumorous disc, spg13, Chaperonin Complexes, DmelCG3576, biodegradation, hirip4, ATP Requiring Protease, hsp60, tend, HIRIP4, chaperonin, Protein Gene Products, ATP Dependent Proteases, plan specification, Gene Proteins, breakdown of substance, CG14724, Bacterium coli commune, DEL, DmelCG5504, SSKS, Bra, hLON"],"pubmed_title_synonyms":["biochemical pathways, Alkalescens-Dispar Group, cellular breakdown, Diffusely Adherent Escherichia coli, Bacterium coli, Escherichia/Shigella coli, biodegradation, Enteroinvasive E. coli, degradation, Peptidomics, breakdown of chemical, catabolism, bacterium E3, E coli, EAggEC, Enteroaggregative E. coli, E. coli., cellular catabolism, Eschericia coli, Enteroaggregative Escherichia coli, breakdown of substance, Bacterium coli commune, Lon Protease, Diffusely Adherent E. coli, Bacillus coli, Escherchia coli, cellular degradation, biotransformation, secretion, Enteroinvasive Escherichia coli, Enterococcus coli, breakdown of molecule, Endopeptidase La"],"description_synonyms":["strain, determination, chemical analysis, Strain, Sprain, Strain., total expressed protein, cultivar, assay, Strains, Sprains, Strains and Sprains, Proteomes, ecotype"],"additional_accession":[]},"is_claimable":false,"name":"Shotgun Proteomics Revealed Preferential Degradation of Misfolded In Vivo Obligate GroE Substrates by Lon Protease in Escherichia coli","description":"Proteome analysis of a conditional GroE expression strain and its variants. Proteome data for the dnaKJ-deleted strain and its variant were also included. ","dates":{"publication":"Mon Jun 27 00:00:00 BST 2022"},"accession":"PXD033134","cross_references":{"TAXONOMY":["562"],"pubmed":["35744894"]}}