{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T10:54:40Z","timestamp":1782989680654,"version":"3.54.5"},"reference-count":102,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,5,1]],"date-time":"2026-05-01T00:00:00Z","timestamp":1777593600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,3,11]],"date-time":"2026-03-11T00:00:00Z","timestamp":1773187200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["AI088075"],"award-info":[{"award-number":["AI088075"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["Al153197"],"award-info":[{"award-number":["Al153197"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2026,5]]},"DOI":"10.1016\/j.jbc.2026.111373","type":"journal-article","created":{"date-parts":[[2026,3,16]],"date-time":"2026-03-16T15:53:10Z","timestamp":1773676390000},"page":"111373","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"title":["Fred Goldberg machines in the pathogenesis of Mycobacterium tuberculosis"],"prefix":"10.1016","volume":"302","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5043-7548","authenticated-orcid":false,"given":"K. Heran","family":"Darwin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jbc.2026.111373_bib1","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1164\/rccm.202011-4239PP","article-title":"Latent tuberculosis: two centuries of confusion","volume":"204","author":"Behr","year":"2021","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"10.1016\/j.jbc.2026.111373_bib2","series-title":"Global Tuberculosis Report 2024","year":"2024"},{"key":"10.1016\/j.jbc.2026.111373_bib3","doi-asserted-by":"crossref","first-page":"5550","DOI":"10.1073\/pnas.84.16.5550","article-title":"Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La","volume":"84","author":"Hwang","year":"1987","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111373_bib4","doi-asserted-by":"crossref","first-page":"4477","DOI":"10.1016\/S0021-9258(18)61217-7","article-title":"A multiple-component, ATP-dependent protease from Escherichia coli","volume":"262","author":"Katayama-Fujimura","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111373_bib5","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.sbi.2020.09.012","article-title":"Structural determinants of regulated proteolysis in pathogenic bacteria by ClpP and the proteasome","volume":"67","author":"Kahne","year":"2021","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.jbc.2026.111373_bib6","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1007\/s003350010173","article-title":"Human and mouse mitochondrial orthologs of bacterial ClpX","volume":"11","author":"Corydon","year":"2000","journal-title":"Mamm. Genome"},{"key":"10.1016\/j.jbc.2026.111373_bib7","doi-asserted-by":"crossref","first-page":"12546","DOI":"10.1016\/S0021-9258(19)38379-6","article-title":"Clp P represents a unique family of serine proteases","volume":"265","author":"Maurizi","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111373_bib8","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1146\/annurev-biochem-060408-172623","article-title":"AAA+ proteases: ATP-fueled machines of protein destruction","volume":"80","author":"Sauer","year":"2011","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.jbc.2026.111373_bib9","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1016\/S1097-2765(03)00060-1","article-title":"Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals","volume":"11","author":"Flynn","year":"2003","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.111373_bib10","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.cell.2019.05.002","article-title":"Alanine tails signal proteolysis in bacterial ribosome-associated quality control","volume":"178","author":"Lytvynenko","year":"2019","journal-title":"Cell"},{"key":"10.1016\/j.jbc.2026.111373_bib11","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1038\/nature20122","article-title":"Arginine phosphorylation marks proteins for degradation by a Clp protease","volume":"539","author":"Trentini","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111373_bib12","doi-asserted-by":"crossref","DOI":"10.1128\/spectrum.02042-22","article-title":"Identification of arginine phosphorylation in Mycolicibacterium Smegmatis","volume":"10","author":"Ogbonna","year":"2022","journal-title":"Microbiol. Spectr."},{"key":"10.1016\/j.jbc.2026.111373_bib13","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1111\/j.1365-2958.2009.06666.x","article-title":"ClpS is the recognition component for Escherichia coli substrates of the N-end rule degradation pathway","volume":"72","author":"Schmidt","year":"2009","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib14","first-page":"990","article-title":"Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger","volume":"271","author":"Keiler","year":"1996","journal-title":"RNA Sci."},{"key":"10.1016\/j.jbc.2026.111373_bib15","doi-asserted-by":"crossref","first-page":"E4587","DOI":"10.1073\/pnas.1417120111","article-title":"Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery","volume":"111","author":"Schmitz","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111373_bib16","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1038\/nm1306","article-title":"Dysregulation of bacterial proteolytic machinery by a new class of antibiotics","volume":"11","author":"Brotz-Oesterhelt","year":"2005","journal-title":"Nat. Med."},{"key":"10.1016\/j.jbc.2026.111373_bib17","doi-asserted-by":"crossref","first-page":"1529","DOI":"10.1038\/emboj.2012.5","article-title":"The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring","volume":"31","author":"Akopian","year":"2012","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2026.111373_bib18","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0125345","article-title":"The Mycobacterium tuberculosis ClpP1P2 protease interacts asymmetrically with its ATPase partners ClpX and ClpC1","volume":"10","author":"Leodolter","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2026.111373_bib19","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002511","article-title":"Mycobacterium tuberculosis ClpP1 and ClpP2 function together in protein degradation and are required for viability in vitro and during infection","volume":"8","author":"Raju","year":"2012","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2026.111373_bib20","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1046\/j.1365-2958.2003.03425.x","article-title":"Genes required for mycobacterial growth defined by high density mutagenesis","volume":"48","author":"Sassetti","year":"2003","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib21","article-title":"The essential M. tuberculosis clp protease is functionally asymmetric in vivo","volume":"8","author":"d'Andrea","year":"2022","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2026.111373_bib22","doi-asserted-by":"crossref","DOI":"10.1038\/nmicrobiol.2016.274","article-title":"Programmable transcriptional repression in mycobacteria using an orthogonal CRISPR interference platform","volume":"2","author":"Rock","year":"2017","journal-title":"Nat. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib23","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1111\/j.1365-2958.2006.05128.x","article-title":"Self-compartmentalized bacterial proteases and pathogenesis","volume":"60","author":"Butler","year":"2006","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib24","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.tube.2013.09.007","article-title":"Mycobacterium tuberculosis possesses an unusual tmRNA rescue system","volume":"94","author":"Personne","year":"2014","journal-title":"Tuberculosis (Edinb)"},{"key":"10.1016\/j.jbc.2026.111373_bib25","doi-asserted-by":"crossref","first-page":"9455","DOI":"10.1074\/jbc.RA120.013456","article-title":"The unfoldase ClpC1 of Mycobacterium tuberculosis regulates the expression of a distinct subset of proteins having intrinsically disordered termini","volume":"295","author":"Lunge","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111373_bib26","doi-asserted-by":"crossref","DOI":"10.1371\/annotation\/bf95b2c0-4085-417b-a2b2-7a85ffe77a9e","article-title":"Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis","volume":"5","author":"Festa","year":"2010","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2026.111373_bib27","doi-asserted-by":"crossref","first-page":"830","DOI":"10.1038\/nsmb814","article-title":"An unstructured initiation site is required for efficient proteasome-mediated degradation","volume":"11","author":"Prakash","year":"2004","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.111373_bib28","doi-asserted-by":"crossref","first-page":"6","DOI":"10.3389\/fmicb.2015.00006","article-title":"Phosphoproteomics analysis of a clinical Mycobacterium tuberculosis Beijing isolate: expanding the mycobacterial phosphoproteome catalog","volume":"6","author":"Fortuin","year":"2015","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib29","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1038\/s41564-022-01313-7","article-title":"The Mycobacterium tuberculosis protein O-phosphorylation landscape","volume":"8","author":"Frando","year":"2023","journal-title":"Nat. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib30","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/S0076-6879(00)28390-0","article-title":"A bacterial two-hybrid system that exploits a cAMP signaling cascade in Escherichia coli","volume":"328","author":"Karimova","year":"2000","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.jbc.2026.111373_bib31","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1111\/febs.15335","article-title":"Genome-wide interaction screen for Mycobacterium tuberculosis ClpCP protease reveals toxin-antitoxin systems as a major substrate class","volume":"288","author":"Ziemski","year":"2021","journal-title":"FEBS J."},{"key":"10.1016\/j.jbc.2026.111373_bib32","doi-asserted-by":"crossref","DOI":"10.3389\/fmolb.2021.691399","article-title":"Control of toxin-antitoxin systems by proteases in mycobacterium Tuberculosis","volume":"8","author":"Bordes","year":"2021","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.jbc.2026.111373_bib33","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1038\/nrmicro1147","article-title":"Prokaryotic toxin-antitoxin stress response loci","volume":"3","author":"Gerdes","year":"2005","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib34","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.aba6944","article-title":"VapBC22 toxin-antitoxin system from Mycobacterium tuberculosis is required for pathogenesis and modulation of host immune response","volume":"6","author":"Agarwal","year":"2020","journal-title":"Sci. Adv."},{"key":"10.1016\/j.jbc.2026.111373_bib35","doi-asserted-by":"crossref","first-page":"5467","DOI":"10.1038\/s41467-024-49246-5","article-title":"Mycobacterium tuberculosis strain with deletions in menT3 and menT4 is attenuated and confers protection in mice and Guinea pigs","volume":"15","author":"Gosain","year":"2024","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.111373_bib36","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1093\/infdis\/jiy109","article-title":"System-Wide analysis unravels the differential regulation and in vivo essentiality of virulence-associated proteins B and C toxin-antitoxin systems of Mycobacterium tuberculosis","volume":"217","author":"Agarwal","year":"2018","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.jbc.2026.111373_bib37","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1038\/scientificamerican0101-68","article-title":"The cellular chamber of doom","volume":"284","author":"Goldberg","year":"2001","journal-title":"Sci. Am."},{"key":"10.1016\/j.jbc.2026.111373_bib38","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1038\/31159","article-title":"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence","volume":"393","author":"Cole","year":"1998","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111373_bib39","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1126\/science.7725097","article-title":"Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution","volume":"268","author":"Lowe","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.111373_bib40","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1126\/science.7725107","article-title":"Proteasome from Thermoplasma acidophilum: a threonine protease","volume":"268","author":"Seemuller","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.111373_bib41","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1038\/386463a0","article-title":"Structure of 20S proteasome from yeast at 2.4 A resolution","volume":"386","author":"Groll","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111373_bib42","doi-asserted-by":"crossref","first-page":"5448","DOI":"10.1128\/JB.180.20.5448-5453.1998","article-title":"The 20S proteasome of Streptomyces coelicolor","volume":"180","author":"Nagy","year":"1998","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jbc.2026.111373_bib43","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1111\/j.1365-2958.2005.05035.x","article-title":"Mycobacterium tuberculosis prcBA genes encode a gated proteasome with broad oligopeptide specificity","volume":"59","author":"Lin","year":"2006","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib44","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1046\/j.1365-2958.1997.4721837.x","article-title":"Inactivation of the 20S proteasome in Mycobacterium smegmatis","volume":"25","author":"Knipfer","year":"1997","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib45","doi-asserted-by":"crossref","first-page":"1963","DOI":"10.1126\/science.1091176","article-title":"The proteasome of Mycobacterium tuberculosis is required for resistance to nitric oxide","volume":"302","author":"Darwin","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.111373_bib46","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1111\/j.1365-2958.2004.04403.x","article-title":"Characterization of a Mycobacterium tuberculosis proteasomal ATPase homologue","volume":"55","author":"Darwin","year":"2005","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib47","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1186\/1745-6150-3-45","article-title":"Unraveling the biochemistry and provenance of pupylation: a prokaryotic analog of ubiquitination","volume":"3","author":"Iyer","year":"2008","journal-title":"Biol. Direct"},{"key":"10.1016\/j.jbc.2026.111373_bib48","doi-asserted-by":"crossref","first-page":"1262","DOI":"10.1038\/emboj.2010.23","article-title":"The mycobacterial Mpa-proteasome unfolds and degrades pupylated substrates by engaging Pup's N-terminus","volume":"29","author":"Striebel","year":"2010","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2026.111373_bib49","doi-asserted-by":"crossref","first-page":"1377","DOI":"10.1016\/j.str.2009.08.010","article-title":"Structural insights on the Mycobacterium tuberculosis proteasomal ATPase Mpa","volume":"17","author":"Wang","year":"2009","journal-title":"Structure"},{"key":"10.1016\/j.jbc.2026.111373_bib50","doi-asserted-by":"crossref","first-page":"1352","DOI":"10.1038\/nsmb.1918","article-title":"Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation","volume":"17","author":"Wang","year":"2010","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.111373_bib51","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1111\/mmi.13695","article-title":"Mycobacterium tuberculosis proteasomal ATPase Mpa has a beta-grasp domain that hinders docking with the proteasome core protease","volume":"05","author":"Wu","year":"2017","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib52","doi-asserted-by":"crossref","DOI":"10.1128\/msphere.00274-22","article-title":"The beta-grasp domain of proteasomal ATPase mpa makes critical contacts with the Mycobacterium tuberculosis 20S core particle to facilitate degradation","volume":"7","author":"Xiao","year":"2022","journal-title":"mSphere"},{"key":"10.1016\/j.jbc.2026.111373_bib53","doi-asserted-by":"crossref","first-page":"4412","DOI":"10.1074\/jbc.M110.189282","article-title":"Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated pup intermediate","volume":"286","author":"Guth","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111373_bib54","doi-asserted-by":"crossref","first-page":"1104","DOI":"10.1126\/science.1163885","article-title":"Ubiquitin-like protein involved in the proteasome pathway of Mycobacterium tuberculosis","volume":"322","author":"Pearce","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.jbc.2026.111373_bib55","doi-asserted-by":"crossref","first-page":"3069","DOI":"10.1074\/jbc.M808032200","article-title":"Proteasomal protein degradation in Mycobacteria is dependent upon a prokaryotic ubiquitin-like protein","volume":"284","author":"Burns","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111373_bib56","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1146\/annurev-cellbio-100617-062802","article-title":"Principles of ubiquitin-dependent signaling","volume":"34","author":"Oh","year":"2018","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"10.1016\/j.jbc.2026.111373_bib57","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.jmb.2009.07.018","article-title":"Prokaryotic ubiquitin-like protein pup is intrinsically disordered","volume":"392","author":"Chen","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.111373_bib58","doi-asserted-by":"crossref","first-page":"3151","DOI":"10.1016\/j.febslet.2009.09.020","article-title":"A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa","volume":"583","author":"Sutter","year":"2009","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2026.111373_bib59","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1038\/nsmb.1597","article-title":"Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes","volume":"16","author":"Striebel","year":"2009","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.111373_bib60","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1146\/annurev-micro-091014-104201","article-title":"Bacterial proteasomes","volume":"69","author":"Jastrab","year":"2015","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib61","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1038\/embor.2010.119","article-title":"Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway","volume":"11","author":"Imkamp","year":"2010","journal-title":"EMBO Rep."},{"key":"10.1016\/j.jbc.2026.111373_bib62","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1016\/j.molcel.2010.07.019","article-title":"\"Depupylation\" of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates","volume":"39","author":"Burns","year":"2010","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.111373_bib63","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1111\/j.1365-2958.2010.07276.x","article-title":"Molecular analysis of the prokaryotic ubiquitin-like protein (Pup) conjugation pathway in Mycobacterium tuberculosis","volume":"77","author":"Cerda-Maira","year":"2010","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib64","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1111\/mmi.15312","article-title":"Tag recycling in the pup-proteasome system is essential for Mycobacterium smegmatis survival under starvation conditions","volume":"122","author":"Zerbib","year":"2024","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib65","doi-asserted-by":"crossref","first-page":"1014","DOI":"10.1038\/ncomms2009","article-title":"Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway","volume":"3","author":"Ozcelik","year":"2012","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.111373_bib66","doi-asserted-by":"crossref","first-page":"4044","DOI":"10.1074\/jbc.M116.755645","article-title":"Depupylase dop requires inorganic phosphate in the active site for catalysis","volume":"292","author":"Bolten","year":"2017","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111373_bib67","doi-asserted-by":"crossref","first-page":"6635","DOI":"10.1038\/s41467-021-26848-x","article-title":"Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation","volume":"12","author":"Cui","year":"2021","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.111373_bib68","doi-asserted-by":"crossref","first-page":"37522","DOI":"10.1074\/jbc.M112.384784","article-title":"Mycobacterium tuberculosis prokaryotic ubiquitin-like protein-deconjugating enzyme is an unusual aspartate amidase","volume":"287","author":"Burns","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111373_bib69","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.00122-17","article-title":"Mycobacterium tuberculosis proteasome accessory factor A (Pafa) can transfer prokaryotic ubiquitin-like protein (Pup) between substrates","volume":"8","author":"Zhang","year":"2017","journal-title":"Mbio"},{"key":"10.1016\/j.jbc.2026.111373_bib70","doi-asserted-by":"crossref","first-page":"668","DOI":"10.1016\/j.jmb.2018.01.009","article-title":"Proteasome accessory factor A (PafA) transferase activity makes sense in the light of its homology with glutamine synthetase","volume":"430","author":"Hecht","year":"2018","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jbc.2026.111373_bib71","doi-asserted-by":"crossref","first-page":"386","DOI":"10.1038\/msb.2010.39","article-title":"Proteome-wide identification of mycobacterial pupylation targets","volume":"6","author":"Poulsen","year":"2010","journal-title":"Mol. Syst. Biol."},{"key":"10.1016\/j.jbc.2026.111373_bib72","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1039\/B916104J","article-title":"Expansion of the mycobacterial \"PUPylome\"","volume":"6","author":"Watrous","year":"2010","journal-title":"Mol. Biosyst."},{"key":"10.1016\/j.jbc.2026.111373_bib73","doi-asserted-by":"crossref","first-page":"5243","DOI":"10.1073\/pnas.94.10.5243","article-title":"Identification of nitric oxide synthase as a protective locus against Tuberculosis","volume":"94","author":"MacMicking","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111373_bib74","doi-asserted-by":"crossref","first-page":"984","DOI":"10.1016\/j.molcel.2015.01.024","article-title":"Proteasomal control of cytokinin synthesis protects Mycobacterium tuberculosis against nitric oxide","volume":"57","author":"Samanovic","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jbc.2026.111373_bib75","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/j.tplants.2014.04.001","article-title":"Cytokinins for immunity beyond growth, galls and green islands","volume":"19","author":"Naseem","year":"2014","journal-title":"Trends Plant Sci."},{"key":"10.1016\/j.jbc.2026.111373_bib76","doi-asserted-by":"crossref","DOI":"10.1128\/mbio.00363-23","article-title":"Aldehyde accumulation in Mycobacterium tuberculosis with defective proteasomal degradation results in copper sensitivity","author":"Limon","year":"2023","journal-title":"mBio"},{"key":"10.1016\/j.jbc.2026.111373_bib77","doi-asserted-by":"crossref","first-page":"3202","DOI":"10.1073\/pnas.1819468116","article-title":"The Mycobacterium tuberculosis Pup-proteasome system regulates nitrate metabolism through an essential protein quality control pathway","volume":"116","author":"Becker","year":"2019","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111373_bib78","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.01545-20","article-title":"Mycobacterium tuberculosis Rv0991c is a Redox-regulated molecular chaperone","author":"Becker","year":"2020","journal-title":"Mbio"},{"key":"10.1016\/j.jbc.2026.111373_bib79","doi-asserted-by":"crossref","first-page":"3129","DOI":"10.1099\/00221287-148-10-3129","article-title":"Dissection of the heat-shock response in Mycobacterium tuberculosis using mutants and microarrays","volume":"148","author":"Stewart","year":"2002","journal-title":"Microbiology"},{"key":"10.1016\/j.jbc.2026.111373_bib80","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/j.tube.2015.03.013","article-title":"The mycobacterial PhoH2 proteins are type II toxin antitoxins coupled to RNA helicase domains","volume":"95","author":"Andrews","year":"2015","journal-title":"Tuberculosis (Edinb)"},{"key":"10.1016\/j.jbc.2026.111373_bib81","doi-asserted-by":"crossref","first-page":"4039","DOI":"10.1002\/1873-3468.13280","article-title":"Biochemical characterization of mt-PemIK, a novel toxin-antitoxin system in Mycobacterium tuberculosis","volume":"592","author":"Chi","year":"2018","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jbc.2026.111373_bib82","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2022136118","article-title":"Mycobacterium tuberculosis VapC4 toxin engages small ORFs to initiate an integrated oxidative and copper stress response","volume":"118","author":"Barth","year":"2021","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111373_bib83","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1111\/mmi.14498","article-title":"Polycysteine-encoding leaderless short ORFs function as cysteine-responsive attenuators of operonic gene expression in mycobacteria","volume":"114","author":"Canestrari","year":"2020","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib84","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1086\/508288","article-title":"Deletion of a Mycobacterium tuberculosis proteasomal ATPase homologue gene produces a slow-growing strain that persists in host tissues","volume":"194","author":"Lamichhane","year":"2006","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.jbc.2026.111373_bib85","doi-asserted-by":"crossref","first-page":"1515","DOI":"10.1038\/nm1683","article-title":"In vivo gene silencing identifies the Mycobacterium tuberculosis proteasome as essential for the bacteria to persist in mice","volume":"13","author":"Gandotra","year":"2007","journal-title":"Nat. Med."},{"key":"10.1016\/j.jbc.2026.111373_bib86","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1001040","article-title":"The Mycobacterium tuberculosis proteasome active site threonine is essential for persistence yet dispensable for replication and resistance to nitric oxide","volume":"6","author":"Gandotra","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.jbc.2026.111373_bib87","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0114348","article-title":"Bacterial proteasome activator bpa (rv3780) is a novel ring-shaped interactor of the mycobacterial proteasome","volume":"9","author":"Delley","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.jbc.2026.111373_bib88","doi-asserted-by":"crossref","first-page":"E1763","DOI":"10.1073\/pnas.1423319112","article-title":"An adenosine triphosphate-independent proteasome activator contributes to the virulence of Mycobacterium Tuberculosis","volume":"112","author":"Jastrab","year":"2015","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111373_bib89","doi-asserted-by":"crossref","first-page":"E1983","DOI":"10.1073\/pnas.1512094113","article-title":"Structural analysis of the dodecameric proteasome activator PafE in Mycobacterium Tuberculosis","volume":"113","author":"Bai","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111373_bib90","doi-asserted-by":"crossref","first-page":"4713","DOI":"10.1074\/jbc.RA117.001471","article-title":"Proteasome substrate capture and gate opening by the accessory factor PafE from Mycobacterium Tuberculosis","volume":"293","author":"Hu","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jbc.2026.111373_bib91","doi-asserted-by":"crossref","DOI":"10.26508\/lsa.202301923","article-title":"ATP-independent substrate recruitment to proteasomal degradation in mycobacteria","volume":"6","author":"von Rosen","year":"2023","journal-title":"Life Sci. Alliance"},{"key":"10.1016\/j.jbc.2026.111373_bib92","doi-asserted-by":"crossref","first-page":"3042","DOI":"10.1038\/s41467-025-58073-1","article-title":"Substrates bind to residues lining the ring of asymmetrically engaged bacterial proteasome activator Bpa","volume":"16","author":"von Rosen","year":"2025","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jbc.2026.111373_bib93","doi-asserted-by":"crossref","first-page":"5423","DOI":"10.1038\/sj.emboj.7601405","article-title":"Identification of substrates of the Mycobacterium tuberculosis proteasome","volume":"25","author":"Pearce","year":"2006","journal-title":"EMBO J."},{"key":"10.1016\/j.jbc.2026.111373_bib94","doi-asserted-by":"crossref","DOI":"10.1128\/JB.00850-16","article-title":"Loss-of-Function mutations in HspR rescue the growth defect of a Mycobacterium tuberculosis proteasome accessory factor E (pafE) mutant","volume":"199","author":"Jastrab","year":"2017","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jbc.2026.111373_bib95","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1038\/89113","article-title":"Overexpression of heat-shock proteins reduces survival of Mycobacterium tuberculosis in the chronic phase of infection","volume":"7","author":"Stewart","year":"2001","journal-title":"Nat. Med."},{"key":"10.1016\/j.jbc.2026.111373_bib96","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1038\/nature08357","article-title":"Inhibitors selective for mycobacterial versus human proteasomes","volume":"461","author":"Lin","year":"2009","journal-title":"Nature"},{"key":"10.1016\/j.jbc.2026.111373_bib97","doi-asserted-by":"crossref","first-page":"6262","DOI":"10.1021\/acs.jmedchem.1c00296","article-title":"Macrocyclic peptides that selectively inhibit the mycobacterium Tuberculosis Proteasome","volume":"64","author":"Zhang","year":"2021","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.jbc.2026.111373_bib98","doi-asserted-by":"crossref","first-page":"2056","DOI":"10.1002\/cbic.201200460","article-title":"Synthesis and evaluation of a selective fluorogenic pup derived assay reagent for Dop, a potential drug target in Mycobacterium tuberculosis","volume":"13","author":"Merkx","year":"2012","journal-title":"Chembiochem"},{"key":"10.1016\/j.jbc.2026.111373_bib99","doi-asserted-by":"crossref","first-page":"3082","DOI":"10.1002\/cbic.202100333","article-title":"Development of tyrphostin analogues to study inhibition of the Mycobacterium tuberculosis Pup proteasome system","volume":"22","author":"Janssen","year":"2021","journal-title":"Chembiochem"},{"key":"10.1016\/j.jbc.2026.111373_bib100","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2407239121","article-title":"Identification of a depupylation regulator for an essential enzyme in Mycobacterium Tuberculosis","volume":"121","author":"Kahne","year":"2024","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.jbc.2026.111373_bib101","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1038\/s41564-022-01073-4","article-title":"ClpP inhibitors are produced by a widespread family of bacterial gene clusters","volume":"7","author":"Culp","year":"2022","journal-title":"Nat. Microbiol."},{"key":"10.1016\/j.jbc.2026.111373_bib102","doi-asserted-by":"crossref","first-page":"113","DOI":"10.7164\/antibiotics.44.113","article-title":"Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells","volume":"44","author":"Omura","year":"1991","journal-title":"J. Antibiot. (Tokyo)"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826002437?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925826002437?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,26]],"date-time":"2026-05-26T23:38:31Z","timestamp":1779838711000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925826002437"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,5]]},"references-count":102,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2026,5]]}},"alternative-id":["S0021925826002437"],"URL":"https:\/\/doi.org\/10.1016\/j.jbc.2026.111373","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2026,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Fred Goldberg machines in the pathogenesis of Mycobacterium tuberculosis","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jbc.2026.111373","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"111373"}}