{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T13:58:10Z","timestamp":1790949490184,"version":"4.1.0"},"reference-count":67,"publisher":"eLife Sciences Publications, Ltd","license":[{"start":{"date-parts":[[2024,4,10]],"date-time":"2024-04-10T00:00:00Z","timestamp":1712707200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2024,4,10]],"date-time":"2024-04-10T00:00:00Z","timestamp":1712707200000},"content-version":"am","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2024,4,10]],"date-time":"2024-04-10T00:00:00Z","timestamp":1712707200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["MO970\/7-1"],"award-info":[{"award-number":["MO970\/7-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elifesciences.org"],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:p>\n                    Heat stress can cause cell death by triggering the aggregation of essential proteins. In bacteria, aggregated proteins are rescued by the canonical Hsp70\/AAA+ (ClpB) bi-chaperone disaggregase. Man-made, severe stress conditions applied during, e.g., food processing represent a novel threat for bacteria by exceeding the capacity of the Hsp70\/ClpB system. Here, we report on the potent autonomous AAA+ disaggregase ClpL from\n                    <jats:italic>Listeria monocytogenes<\/jats:italic>\n                    that provides enhanced heat resistance to the food-borne pathogen enabling persistence in adverse environments. ClpL shows increased thermal stability and enhanced disaggregation power compared to Hsp70\/ClpB, enabling it to withstand severe heat stress and to solubilize tight aggregates. ClpL binds to protein aggregates via aromatic residues present in its N-terminal domain (NTD) that adopts a partially folded and dynamic conformation. Target specificity is achieved by simultaneous interactions of multiple NTDs with the aggregate surface. ClpL shows remarkable structural plasticity by forming diverse higher assembly states through interacting ClpL rings. NTDs become largely sequestered upon ClpL ring interactions. Stabilizing ring assemblies by engineered disulfide bonds strongly reduces disaggregation activity, suggesting that they represent storage states.\n                  <\/jats:p>","DOI":"10.7554\/elife.92746","type":"journal-article","created":{"date-parts":[[2023,11,17]],"date-time":"2023-11-17T08:13:40Z","timestamp":1700208820000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.92746","source":"Crossref","is-referenced-by-count":14,"title":["The Listeria monocytogenes persistence factor ClpL is a potent stand-alone disaggregase"],"prefix":"10.7554","volume":"12","author":[{"given":"Valentin","family":"Bohl","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/038t36y30","id-type":"ROR","asserted-by":"publisher"}],"name":"Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance","place":["Heidelberg, Germany"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"data-curation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"visualization","vocabulary":"credit"}]},{"given":"Nele Merret","family":"Hollmann","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03mstc592","id-type":"ROR","asserted-by":"publisher"}],"name":"Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL) Heidelberg","place":["Heidelberg, Germany"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"data-curation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"}]},{"given":"Tobias","family":"Melzer","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/038t36y30","id-type":"ROR","asserted-by":"publisher"}],"name":"Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance","place":["Heidelberg, Germany"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"data-curation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"}]},{"given":"Panagiotis","family":"Katikaridis","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/038t36y30","id-type":"ROR","asserted-by":"publisher"}],"name":"Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance","place":["Heidelberg, Germany"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"data-curation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"}]},{"given":"Lena","family":"Meins","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/038t36y30","id-type":"ROR","asserted-by":"publisher"}],"name":"Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance","place":["Heidelberg, Germany"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"data-curation","vocabulary":"credit"}]},{"given":"Bernd","family":"Simon","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03mstc592","id-type":"ROR","asserted-by":"publisher"}],"name":"Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL) Heidelberg","place":["Heidelberg, Germany"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"data-curation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"visualization","vocabulary":"credit"}]},{"given":"Dirk","family":"Flemming","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/038t36y30","id-type":"ROR","asserted-by":"publisher"}],"name":"Heidelberg University Biochemistry Center (BZH)","place":["Heidelberg, Germany"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"data-curation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9127-4477","authenticated-orcid":true,"given":"Irmgard","family":"Sinning","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/038t36y30","id-type":"ROR","asserted-by":"publisher"}],"name":"Heidelberg University Biochemistry Center (BZH)","place":["Heidelberg, Germany"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"methodology","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5214-7002","authenticated-orcid":true,"given":"Janosch","family":"Hennig","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03mstc592","id-type":"ROR","asserted-by":"publisher"}],"name":"Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL) Heidelberg","place":["Heidelberg, Germany"]},{"id":[{"id":"https:\/\/ror.org\/0234wmv40","id-type":"ROR","asserted-by":"publisher"}],"name":"Chair of Biochemistry IV, Biophysical Chemistry, University of Bayreuth","place":["Bayreuth, Germany"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"methodology","vocabulary":"credit"},{"role":"visualization","vocabulary":"credit"},{"role":"writing-review-editing","vocabulary":"credit"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3674-5410","authenticated-orcid":true,"given":"Axel","family":"Mogk","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/038t36y30","id-type":"ROR","asserted-by":"publisher"}],"name":"Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance","place":["Heidelberg, Germany"]}],"role":[{"role":"author","vocabulary":"crossref"},{"role":"corresponding-author","vocabulary":"crossref"},{"role":"conceptualization","vocabulary":"credit"},{"role":"data-curation","vocabulary":"credit"},{"role":"formal-analysis","vocabulary":"credit"},{"role":"funding-acquisition","vocabulary":"credit"},{"role":"project-administration","vocabulary":"credit"},{"role":"writing-original-draft","vocabulary":"credit"}]}],"member":"4374","published-online":{"date-parts":[[2024,4,10]]},"reference":[{"key":"bib1","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1007\/s10858-013-9737-7","type":"journal-article","article-title":"PINT: a software for integration of peak volumes and extraction of relaxation rates","volume":"56","author":"Ahlner","year":"2013","journal-title":"Journal of Biomolecular NMR"},{"key":"bib2","doi-asserted-by":"publisher","first-page":"597","DOI":"10.1142\/s0219720006002016","type":"journal-article","article-title":"Trend of amino acid composition of proteins of different taxa","volume":"4","author":"Bogatyreva","year":"2006","journal-title":"Journal of Bioinformatics and Computational Biology"},{"key":"bib3","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0015467","type":"journal-article","article-title":"Heat resistance mediated by a new plasmid encoded Clp ATPase, ClpK, as a possible novel mechanism for nosocomial persistence of Klebsiella pneumoniae","volume":"5","author":"Bojer","year":"2010","journal-title":"PLOS ONE"},{"key":"bib4","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2017.00579","type":"journal-article","article-title":"Turn up the heat-food and Clinical Escherichia coli Isolates feature two transferrable loci of heat resistance","volume":"8","author":"Boll","year":"2017","journal-title":"Frontiers in Microbiology"},{"key":"bib5","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2018.02700","type":"journal-article","article-title":"Resistance of Listeria monocytogenes to stress conditions encountered in food and food processing environments","volume":"9","author":"Bucur","year":"2018","journal-title":"Frontiers in Microbiology"},{"key":"bib6","doi-asserted-by":"publisher","DOI":"10.1016\/j.celrep.2022.111408","type":"journal-article","article-title":"Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3","volume":"40","author":"Cupo","year":"2022","journal-title":"Cell Reports"},{"key":"bib7","doi-asserted-by":"publisher","first-page":"277","DOI":"10.1007\/BF00197809","type":"journal-article","article-title":"NMRPipe: a multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"Journal of Biomolecular NMR"},{"key":"bib8","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.1701726","type":"journal-article","article-title":"Structural pathway of regulated substrate transfer and threading through an Hsp100 disaggregase","volume":"3","author":"Deville","year":"2017","journal-title":"Science Advances"},{"key":"bib9","doi-asserted-by":"publisher","DOI":"10.1038\/s41421-022-00379-1","type":"journal-article","article-title":"Cryo-EM structures of human p97 double hexamer capture potentiated ATPase-competent state","volume":"8","author":"Gao","year":"2022","journal-title":"Cell Discovery"},{"key":"bib10","doi-asserted-by":"publisher","first-page":"808","DOI":"10.1016\/j.molcel.2015.10.021","type":"journal-article","article-title":"Coordinated Ribosomal ITS2 RNA Processing by the Las1 Complex Integrating Endonuclease, Polynucleotide Kinase, and Exonuclease Activities","volume":"60","author":"Gasse","year":"2015","journal-title":"Molecular Cell"},{"key":"bib11","doi-asserted-by":"publisher","DOI":"10.1126\/sciadv.adf5336","type":"journal-article","article-title":"Dodecamer assembly of a metazoan AAA+ chaperone couples substrate extraction to refolding","volume":"9","author":"Gupta","year":"2023","journal-title":"Science Advances"},{"key":"bib12","doi-asserted-by":"publisher","first-page":"641","DOI":"10.1038\/nsmb.1425","type":"journal-article","article-title":"Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments","volume":"15","author":"Haslberger","year":"2008","journal-title":"Nature Structural & Molecular Biology"},{"key":"bib13","doi-asserted-by":"publisher","first-page":"957","DOI":"10.1111\/j.1365-2958.1993.tb01187.x","type":"journal-article","article-title":"Two genes present on a transposon-like structure in Lactococcus lactis are involved in a Clp-family proteolytic activity","volume":"7","author":"Huang","year":"1993","journal-title":"Molecular Microbiology"},{"key":"bib14","doi-asserted-by":"publisher","first-page":"775","DOI":"10.1021\/acschembio.1c00156","type":"journal-article","article-title":"Entropic inhibition: how the activity of a AAA+ machine is modulated by its substrate-binding domain","volume":"16","author":"Iljina","year":"2021","journal-title":"ACS Chemical Biology"},{"key":"bib15","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1016\/j.ijfoodmicro.2015.10.022","type":"journal-article","article-title":"Efflux pump-mediated benzalkonium chloride resistance in Listeria monocytogenes isolated from retail food","volume":"217","author":"Jiang","year":"2016","journal-title":"International Journal of Food Microbiology"},{"key":"bib16","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","type":"journal-article","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"bib17","doi-asserted-by":"publisher","first-page":"255","DOI":"10.1111\/mmi.14614","type":"journal-article","article-title":"A recently isolated human commensal Escherichia coli ST10 clone member mediates enhanced thermotolerance and tetrathionate respiration on A P1 phage-derived IncY plasmid","volume":"115","author":"Kamal","year":"2021","journal-title":"Molecular Microbiology"},{"key":"bib18","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2021.696522","type":"journal-article","article-title":"Horizontal transmission of stress resistance genes shape the ecology of beta- and gamma-proteobacteria","volume":"12","author":"Kamal","year":"2021","journal-title":"Frontiers in Microbiology"},{"key":"bib19","doi-asserted-by":"publisher","DOI":"10.3390\/biom9120815","type":"journal-article","article-title":"ClpG provides increased heat resistance by acting as superior disaggregase","volume":"9","author":"Katikaridis","year":"2019","journal-title":"Biomolecules"},{"key":"bib20","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2023.105336","type":"journal-article","article-title":"Structural basis of aggregate binding by the AAA+ disaggregase ClpG","volume":"299","author":"Katikaridis","year":"2023","journal-title":"The Journal of Biological Chemistry"},{"key":"bib21","doi-asserted-by":"publisher","first-page":"14353","DOI":"10.1096\/fj.202000843R","type":"journal-article","article-title":"ClpL is a functionally active tetradecameric AAA+ chaperone, distinct from hexameric\/dodecameric ones","volume":"34","author":"Kim","year":"2020","journal-title":"FASEB Journal"},{"key":"bib22","doi-asserted-by":"publisher","first-page":"589","DOI":"10.1038\/nrmicro2185","type":"journal-article","article-title":"Adapting the machine: adaptor proteins for Hsp100\/Clp and AAA+ proteases","volume":"7","author":"Kirstein","year":"2009","journal-title":"Nature Reviews. Microbiology"},{"key":"bib23","doi-asserted-by":"publisher","first-page":"3633","DOI":"10.1096\/fj.10-156992","type":"journal-article","article-title":"Independent evolution of the core domain and its flanking sequences in small heat shock proteins","volume":"24","author":"Kriehuber","year":"2010","journal-title":"FASEB Journal"},{"key":"bib24","doi-asserted-by":"publisher","first-page":"3757","DOI":"10.1128\/IAI.71.7.3757-3765.2003","type":"journal-article","article-title":"Effect of heat shock and mutations in ClpL and ClpP on virulence gene expression in Streptococcus pneumoniae","volume":"71","author":"Kwon","year":"2003","journal-title":"Infection and Immunity"},{"key":"bib25","doi-asserted-by":"publisher","first-page":"3040","DOI":"10.1128\/jb.176.10.3040-3048.1994","type":"journal-article","article-title":"Plasmid-borne cadmium resistance genes in Listeria monocytogenes are similar to cadA and cadC of Staphylococcus aureus and are induced by cadmium","volume":"176","author":"Lebrun","year":"1994","journal-title":"Journal of Bacteriology"},{"key":"bib26","doi-asserted-by":"publisher","first-page":"1325","DOI":"10.1093\/bioinformatics\/btu830","type":"journal-article","article-title":"NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy","volume":"31","author":"Lee","year":"2015","journal-title":"Bioinformatics"},{"key":"bib27","doi-asserted-by":"publisher","first-page":"E273","DOI":"10.1073\/pnas.1712051115","type":"journal-article","article-title":"Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria","volume":"115","author":"Lee","year":"2018","journal-title":"PNAS"},{"key":"bib28","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-023-37657-9","type":"journal-article","article-title":"Structural basis of impaired disaggregase function in the oxidation-sensitive SKD3 mutant causing 3-methylglutaconic aciduria","volume":"14","author":"Lee","year":"2023","journal-title":"Nature Communications"},{"key":"bib29","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0025777","type":"journal-article","article-title":"Transcriptome analysis of adaptive heat shock response of Streptococcus thermophilus","volume":"6","author":"Li","year":"2011","journal-title":"PLOS ONE"},{"key":"bib30","doi-asserted-by":"publisher","first-page":"2857","DOI":"10.1074\/jbc.M112.387589","type":"journal-article","article-title":"Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70","volume":"288","author":"Lipi\u0144ska","year":"2013","journal-title":"The Journal of Biological Chemistry"},{"key":"bib31","doi-asserted-by":"publisher","DOI":"10.3791\/2574","type":"journal-article","article-title":"Single particle electron microscopy reconstruction of the exosome complex using the random conical tilt method","volume":"01","author":"Liu","year":"2011","journal-title":"Journal of Visualized Experiments"},{"key":"bib32","doi-asserted-by":"publisher","first-page":"276","DOI":"10.1111\/j.1472-765X.2007.02305.x","type":"journal-article","article-title":"Acid and heat tolerance of persistent and nonpersistent Listeria monocytogenes food plant strains","volume":"46","author":"Lund\u00e9n","year":"2008","journal-title":"Letters in Applied Microbiology"},{"key":"bib33","doi-asserted-by":"publisher","first-page":"1169","DOI":"10.1016\/j.chembiol.2019.05.008","type":"journal-article","article-title":"Toxic Activation of an AAA+ Protease by the Antibacterial Drug Cyclomarin A","volume":"26","author":"Maurer","year":"2019","journal-title":"Cell Chemical Biology"},{"key":"bib34","doi-asserted-by":"publisher","first-page":"679","DOI":"10.1038\/s41592-022-01488-1","type":"journal-article","article-title":"ColabFold: making protein folding accessible to all","volume":"19","author":"Mirdita","year":"2022","journal-title":"Nature Methods"},{"key":"bib35","doi-asserted-by":"publisher","first-page":"6934","DOI":"10.1093\/emboj\/18.24.6934","type":"journal-article","article-title":"Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB","volume":"18","author":"Mogk","year":"1999","journal-title":"The EMBO Journal"},{"key":"bib36","doi-asserted-by":"publisher","first-page":"17615","DOI":"10.1074\/jbc.M209686200","type":"journal-article","article-title":"Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity","volume":"278","author":"Mogk","year":"2003","journal-title":"The Journal of Biological Chemistry"},{"key":"bib37","doi-asserted-by":"publisher","first-page":"2338","DOI":"10.1016\/j.cell.2022.05.009","type":"journal-article","article-title":"BacPROTACs mediate targeted protein degradation in bacteria","volume":"185","author":"Morreale","year":"2022","journal-title":"Cell"},{"key":"bib38","doi-asserted-by":"publisher","first-page":"39","DOI":"10.1016\/j.ijfoodmicro.2019.03.016","type":"journal-article","article-title":"Plasmids contribute to food processing environment-associated stress survival in three Listeria monocytogenes ST121, ST8, and ST5 strains","volume":"299","author":"Naditz","year":"2019","journal-title":"International Journal of Food Microbiology"},{"key":"bib39","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1007\/s10858-017-0141-6","type":"journal-article","article-title":"Comprehensive analysis of NMR data using advanced line shape fitting","volume":"69","author":"Niklasson","year":"2017","journal-title":"Journal of Biomolecular NMR"},{"key":"bib40","doi-asserted-by":"publisher","first-page":"1338","DOI":"10.1038\/nsmb.2441","type":"journal-article","article-title":"A tightly regulated molecular toggle controls AAA+ disaggregase","volume":"19","author":"Oguchi","year":"2012","journal-title":"Nature Structural & Molecular Biology"},{"key":"bib41","doi-asserted-by":"crossref","first-page":"5279","DOI":"10.1016\/S0021-9258(18)42763-9","type":"journal-article","article-title":"DnaK, hsp73, and their molten globules: two different ways heat shock proteins respond to heat","volume":"267","author":"Palleros","year":"1992","journal-title":"The Journal of Biological Chemistry"},{"key":"bib42","doi-asserted-by":"publisher","first-page":"1352","DOI":"10.1111\/febs.13228","type":"journal-article","article-title":"ClpL is a chaperone without auxiliary factors","volume":"282","author":"Park","year":"2015","journal-title":"The FEBS Journal"},{"key":"bib43","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2021.796040","type":"journal-article","article-title":"Virulence and Antibiotic Resistance Genes in Listeria monocytogenes Strains Isolated From Ready-to-Eat Foods in Chile","volume":"12","author":"Parra-Flores","year":"2021","journal-title":"Frontiers in Microbiology"},{"key":"bib44","doi-asserted-by":"publisher","DOI":"10.1128\/mSphere.00364-17","type":"journal-article","article-title":"Heat Resistance Mediated by pLM58 Plasmid-Borne ClpL in Listeria monocytogenes","volume":"2","author":"P\u00f6ntinen","year":"2017","journal-title":"mSphere"},{"key":"bib45","doi-asserted-by":"publisher","first-page":"1422","DOI":"10.1016\/0140-6736(90)91447-i","type":"journal-article","article-title":"Transferable plasmid-mediated antibiotic resistance in Listeria monocytogenes","volume":"335","author":"Poyart-Salmeron","year":"1990","journal-title":"Lancet"},{"key":"bib46","doi-asserted-by":"publisher","first-page":"43","DOI":"10.1038\/s41580-019-0183-6","type":"journal-article","article-title":"The molecular principles governing the activity and functional diversity of AAA+ proteins","volume":"21","author":"Puchades","year":"2020","journal-title":"Nature Reviews. Molecular Cell Biology"},{"key":"bib47","doi-asserted-by":"publisher","DOI":"10.3389\/fmicb.2023.1160244","type":"journal-article","article-title":"Whole-genome sequencing of Listeria innocua recovered from retail milk and dairy products in Egypt","volume":"14","author":"Ramadan","year":"2023","journal-title":"Frontiers in Microbiology"},{"key":"bib48","doi-asserted-by":"publisher","first-page":"E6872","DOI":"10.1073\/pnas.1512783112","type":"journal-article","article-title":"ClpB N-terminal domain plays a regulatory role in protein disaggregation","volume":"112","author":"Rosenzweig","year":"2015","journal-title":"PNAS"},{"key":"bib49","doi-asserted-by":"publisher","first-page":"93","DOI":"10.1016\/S0079-6565(98)00025-9","type":"journal-article","article-title":"Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients","volume":"34","author":"Sattler","year":"1999","journal-title":"Progress in Nuclear Magnetic Resonance Spectroscopy"},{"key":"bib50","doi-asserted-by":"publisher","first-page":"1347","DOI":"10.1038\/nsmb.2442","type":"journal-article","article-title":"Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces","volume":"19","author":"Seyffer","year":"2012","journal-title":"Nature Structural & Molecular Biology"},{"key":"bib51","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.202202149","type":"journal-article","article-title":"The cytoprotective sequestration activity of small heat shock proteins is evolutionarily conserved","volume":"221","author":"Shrivastava","year":"2022","journal-title":"The Journal of Cell Biology"},{"key":"bib52","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1007\/s10858-019-00243-7","type":"journal-article","article-title":"Improving the sensitivity of FT-NMR spectroscopy by apodization weighted sampling","volume":"73","author":"Simon","year":"2019","journal-title":"Journal of Biomolecular NMR"},{"key":"bib53","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1016\/j.bbrc.2022.02.101","type":"journal-article","article-title":"Human mitochondrial AAA+ ATPase SKD3\/CLPB assembles into nucleotide-stabilized dodecamers","volume":"602","author":"Spaulding","year":"2022","journal-title":"Biochemical and Biophysical Research Communications"},{"key":"bib54","doi-asserted-by":"publisher","first-page":"2061","DOI":"10.1128\/AEM.71.4.2061-2069.2005","type":"journal-article","article-title":"Characterization of a mobile clpL gene from Lactobacillus rhamnosus","volume":"71","author":"Suokko","year":"2005","journal-title":"Applied and Environmental Microbiology"},{"key":"bib55","doi-asserted-by":"publisher","first-page":"1029","DOI":"10.1002\/pmic.200700925","type":"journal-article","article-title":"ClpL is essential for induction of thermotolerance and is potentially part of the HrcA regulon in Lactobacillus gasseri","volume":"8","author":"Suokko","year":"2008","journal-title":"Proteomics"},{"key":"bib56","doi-asserted-by":"publisher","first-page":"9755","DOI":"10.1073\/pnas.95.17.9755","type":"journal-article","article-title":"Biochemical basis of SOS-induced mutagenesis in Escherichia coli: reconstitution of in vitro lesion bypass dependent on the UmuD\u20192C mutagenic complex and RecA protein","volume":"95","author":"Tang","year":"1998","journal-title":"PNAS"},{"key":"bib57","doi-asserted-by":"publisher","first-page":"576","DOI":"10.1128\/JB.01743-12","type":"journal-article","article-title":"ClpL is required for folding of CtsR in Streptococcus mutans","volume":"195","author":"Tao","year":"2013","journal-title":"Journal of Bacteriology"},{"key":"bib58","doi-asserted-by":"publisher","DOI":"10.1016\/j.jbc.2022.102202","type":"journal-article","article-title":"Antibacterial peptide CyclomarinA creates toxicity by deregulating the Mycobacterium tuberculosis ClpC1-ClpP1P2 protease","volume":"298","author":"Taylor","year":"2022","journal-title":"The Journal of Biological Chemistry"},{"key":"bib59","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1006\/jsbi.1996.0004","type":"journal-article","article-title":"A new generation of the IMAGIC image processing system","volume":"116","author":"van Heel","year":"1996","journal-title":"Journal of Structural Biology"},{"key":"bib60","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1307066110","type":"journal-article","article-title":"Distinct quaternary structures of the AAA+ Lon protease control substrate degradation","volume":"110","author":"Vieux","year":"2013","journal-title":"PNAS"},{"key":"bib61","doi-asserted-by":"publisher","first-page":"653","DOI":"10.1016\/j.cell.2004.11.027","type":"journal-article","article-title":"Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB","volume":"119","author":"Weibezahn","year":"2004","journal-title":"Cell"},{"key":"bib62","doi-asserted-by":"publisher","first-page":"178","DOI":"10.1016\/j.jmb.2008.02.026","type":"journal-article","article-title":"Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB","volume":"378","author":"Werbeck","year":"2008","journal-title":"Journal of Molecular Biology"},{"key":"bib63","doi-asserted-by":"publisher","first-page":"387","DOI":"10.1083\/jcb.201201074","type":"journal-article","article-title":"Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation","volume":"198","author":"Winkler","year":"2012","journal-title":"The Journal of Cell Biology"},{"key":"bib64","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1007\/BF00175245","type":"journal-article","article-title":"The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data","volume":"4","author":"Wishart","year":"1994","journal-title":"Journal of Biomolecular NMR"},{"key":"bib65","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.3001987","type":"journal-article","article-title":"Comprehensive structural characterization of the human AAA+ disaggregase CLPB in the apo- and substrate-bound states reveals a unique mode of action driven by oligomerization","volume":"21","author":"Wu","year":"2023","journal-title":"PLOS Biology"},{"key":"bib66","doi-asserted-by":"publisher","first-page":"28083","DOI":"10.1074\/jbc.274.40.28083","type":"journal-article","article-title":"ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation: a novel multi-chaperone system from Escherichia coli","volume":"274","author":"Zolkiewski","year":"1999","journal-title":"The Journal of Biological Chemistry"},{"key":"dataset1","type":"dataset","article-title":"ClpL NTD","volume-title":"BMRB","author":"Hennig","year":"2023","unstructured":"Hennig J. 2023. ClpL NTD. BMRB. https:\/\/bmrb.io\/data_library\/summary\/index.php?bmrbId=52068. 52068."}],"container-title":["eLife"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/cdn.elifesciences.org\/articles\/92746\/elife-92746-v2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/cdn.elifesciences.org\/articles\/92746\/elife-92746-v2.xml","content-type":"application\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/elifesciences.org\/articles\/92746","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,8,24]],"date-time":"2026-08-24T10:36:50Z","timestamp":1787567810000},"score":1,"resource":{"primary":{"URL":"https:\/\/elifesciences.org\/articles\/92746"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,4,10]]},"references-count":67,"alternative-id":["10.7554\/eLife.92746"],"URL":"https:\/\/doi.org\/10.7554\/elife.92746","archive":["CLOCKSS"],"relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2023.10.08.561430","asserted-by":"subject"}],"is-same-as":[{"id-type":"doi","id":"10.7554\/eLife.92746.3","asserted-by":"subject"}],"is-version-of":[{"id-type":"doi","id":"10.7554\/eLife.92746.1","asserted-by":"subject"},{"id-type":"doi","id":"10.7554\/eLife.92746.2","asserted-by":"subject"}],"is-supplemented-by":[{"id-type":"accession","id":"52068","asserted-by":"subject"}]},"ISSN":["2050-084X"],"issn-type":[{"value":"2050-084X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,4,10]]},"assertion":[{"value":"single anonymised","name":"peer_review_transparency","label":"Peer review transparency","group":{"name":"peer_review_taxonomy"}},{"value":"other reviewer(s), editor","name":"peer_review_interaction","label":"Peer review interaction","group":{"name":"peer_review_taxonomy"}},{"value":"review summaries, review reports, author\/editor communication, reviewer identities reviewer opt in, editor identities","name":"peer_review_published","label":"Peer review published","group":{"name":"peer_review_taxonomy"}},{"value":"open (sign in with ORCID iD required)","name":"post_publication_commenting","label":"Post publication commenting","group":{"name":"post_publication_commenting"}}],"article-number":"RP92746"}}