{"entity": "researcher", "timestamp": "2026-09-25T21:28:28.825Z", "family": "Jenne", "given": "Timo", "initials": "T", "orcid": "0009-0001-2033-5102", "affiliations": ["Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 345, Heidelberg, 69120, Germany."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/9225663defb84e03980f7c915decb373.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/9225663defb84e03980f7c915decb373"}}, "publications": [{"entity": "publication", "iuid": "c924c157ac534ce4ac0f021480ed736c", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/c924c157ac534ce4ac0f021480ed736c.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/c924c157ac534ce4ac0f021480ed736c"}}, "title": "Allosteric control of the bacterial ClpC/ClpP protease and its hijacking by antibacterial peptides.", "authors": [{"family": "Jenne", "given": "Timo", "initials": "T", "orcid": "0009-0001-2033-5102", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9225663defb84e03980f7c915decb373.json"}}, {"family": "Engelhardt", "given": "Lisa", "initials": "L", "orcid": "0009-0003-7437-2130", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5f037ea0055e4ba79e4aa43897a22db5.json"}}, {"family": "Baronaite", "given": "Ieva", "initials": "I", "orcid": "0009-0006-5515-8528", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/900d2fdc877649538a1e6bd20cfb1a2e.json"}}, {"family": "Levy", "given": "Dorit", "initials": "D"}, {"family": "Riven", "given": "Inbal", "initials": "I"}, {"family": "Malolepszy", "given": "Maciej", "initials": "M", "orcid": "0009-0000-9501-5990", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/183be476fa6a4e6d9d30ca2c5d29be97.json"}}, {"family": "Azinas", "given": "Stavros", "initials": "S", "orcid": "0000-0002-3744-9229", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/38998c283714477faec7357c3990b4e1.json"}}, {"family": "Sych", "given": "Taras", "initials": "T"}, {"family": "Sezgin", "given": "Erdinc", "initials": "E"}, {"family": "Flemming", "given": "Dirk", "initials": "D", "orcid": "0000-0002-1528-5032", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9991c8770bbd4927a283af742282f5a6.json"}}, {"family": "Sinning", "given": "Irmgard", "initials": "I", "orcid": "0000-0001-9127-4477", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e876dacd787949728f5c4f2d51ba51ed.json"}}, {"family": "Haran", "given": "Gilad", "initials": "G", "orcid": "0000-0003-1837-9779", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/dd21744c82b84df1a5d802590e865747.json"}}, {"family": "Carroni", "given": "Marta", "initials": "M", "orcid": "0000-0002-7697-6427", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/55fa4ba347a34d7ca80d214e8d718e44.json"}}, {"family": "Mogk", "given": "Axel", "initials": "A", "orcid": "0000-0003-3674-5410", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/cfd11670a5454183999d1a1765b2a99d.json"}}], "type": "journal article", "published": "2025-11-00", "journal": {"title": "EMBO J.", "issn": "1460-2075", "volume": "44", "issue": "21", "pages": "6273-6296", "issn-l": "0261-4189"}, "abstract": "The hexameric AAA+ protein ClpC, combined with peptidase ClpP, forms a critical ATP-dependent protease in bacteria, essential for virulence. ClpC is usually repressed in an inactive resting state, where two ClpC spirals interact via coiled-coil M-domains. Antibacterial peptides and partner proteins trigger ClpC activation by binding to its N-terminal domain (NTD). This study reveals that the NTD stabilizes the resting state through multiple anchoring points to M-domains and ATPase domains. The same NTD sites also serve as binding sites for adaptor proteins and substrates carrying phosphorylated arginines (pArg), disrupting resting state interactions and promoting active ClpC hexamer formation. This coupling ensures that ClpC activation aligns with substrate and partner protein availability. Toxic peptides exploit this regulatory mechanism, leading to continuous ClpC activation and harmful, uncontrolled proteolysis. These findings highlight the dual role of the NTD in maintaining resting state stability and mediating activation, emphasizing its critical role in bacterial protease regulation and its potential as a drug target.", "doi": "10.1038/s44318-025-00575-1", "pmid": "41023306", "labels": {"SciLifeLab Fellow": "", "Erdinc Sezgin": ""}, "xrefs": [{"db": "pmc", "key": "PMC12583610"}, {"db": "pii", "key": "10.1038/s44318-025-00575-1"}], "notes": [], "created": "2026-09-23T11:37:14.125Z", "modified": "2026-09-23T11:37:14.541Z"}, {"entity": "publication", "iuid": "3c98bfc13be242038a5221273b8a0bdb", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/3c98bfc13be242038a5221273b8a0bdb.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/3c98bfc13be242038a5221273b8a0bdb"}}, "title": "Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP.", "authors": [{"family": "Azinas", "given": "Stavros", "initials": "S", "orcid": "0000-0002-3744-9229", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/38998c283714477faec7357c3990b4e1.json"}}, {"family": "Wallden", "given": "Karin", "initials": "K"}, {"family": "Katikaridis", "given": "Panagiotis", "initials": "P"}, {"family": "Jenne", "given": "Timo", "initials": "T", "orcid": "0009-0001-2033-5102", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9225663defb84e03980f7c915decb373.json"}}, {"family": "Schahl", "given": "Adrien", "initials": "A", "orcid": "0000-0001-5839-7715", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5235b9e0314546949c6454aa3620f50a.json"}}, {"family": "Mogk", "given": "Axel", "initials": "A", "orcid": "0000-0003-3674-5410", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/cfd11670a5454183999d1a1765b2a99d.json"}}, {"family": "Carroni", "given": "Marta", "initials": "M", "orcid": "0000-0002-7697-6427", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/55fa4ba347a34d7ca80d214e8d718e44.json"}}], "type": "journal article", "published": "2025-10-14", "journal": {"title": "Commun Biol", "issn": "2399-3642", "volume": "8", "issue": "1", "pages": "1467", "issn-l": "2399-3642"}, "abstract": "Bacterial AAA+ proteases are composed of a AAA+ partner (e.g., ClpC) and an associated peptidase (e.g., ClpP). They represent ATP-fuelled and self-compartmentalized proteolytic machines that are crucial for stress resistance and virulence. ClpC requires cooperation with adaptor proteins such as MecA for activation and complex formation with ClpP. Here, we present the cryo-EM structure of the MecA/ClpC/ClpP complex from the major pathogen Staphylococcus aureus. MecA forms a dynamic crown on top of the ClpC/ClpP complex with its substrate-binding domain positioned near the ClpC pore site, likely facilitating substrate transfer. ClpC/ClpP complex formation involves ClpC P-loops and ClpP N-terminal \u03b2-hairpins, which insert into the central ClpC threading channel and contact sites next to the ClpC ATPase center. ClpC and ClpP interactions are asymmetric and dictated by the activity states of ClpC ATPase subunits. ClpP binding increases ClpC ATPase and threading activities in a \u03b2-hairpin dependent manner, illuminating an allosteric pathway in the cooperation of ATPase and peptidase components in bacterial AAA+ proteases.", "doi": "10.1038/s42003-025-08908-w", "pmid": "41087538", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC12521514"}, {"db": "pii", "key": "10.1038/s42003-025-08908-w"}], "notes": [], "created": "2026-09-23T11:37:23.089Z", "modified": "2026-09-23T11:37:23.180Z"}, {"entity": "publication", "iuid": "95ec9bf7ceae4e9aa037d25e28c7bd04", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/95ec9bf7ceae4e9aa037d25e28c7bd04.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/95ec9bf7ceae4e9aa037d25e28c7bd04"}}, "title": "Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP", "authors": [{"family": "Azinas", "given": "Stavros", "initials": "S", "orcid": "0000-0002-3744-9229", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/38998c283714477faec7357c3990b4e1.json"}}, {"family": "Wallden", "given": "Karin", "initials": "K"}, {"family": "Katikaridis", "given": "Panagiotis", "initials": "P"}, {"family": "Jenne", "given": "Timo", "initials": "T", "orcid": "0009-0001-2033-5102", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9225663defb84e03980f7c915decb373.json"}}, {"family": "Schahl", "given": "Adrien", "initials": "A", "orcid": "0000-0001-5839-7715", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5235b9e0314546949c6454aa3620f50a.json"}}, {"family": "Mogk", "given": "Axel", "initials": "A", "orcid": "0000-0003-3674-5410", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/cfd11670a5454183999d1a1765b2a99d.json"}}, {"family": "Carroni", "given": "Marta", "initials": "M", "orcid": "0000-0002-7697-6427", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/55fa4ba347a34d7ca80d214e8d718e44.json"}}], "type": "posted-content", "published": "2025-06-06", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/2025.06.06.658286", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-09-23T15:48:08.400Z", "modified": "2026-09-23T15:48:08.482Z"}]}