{"entity": "researcher", "timestamp": "2026-08-20T21:16:22.263Z", "family": "Gilmore", "given": "Michael C", "initials": "MC", "orcid": "0000-0002-6848-5134", "affiliations": ["The Laboratory for Molecular Infection Medicine Sweden, Ume\u00e5 Center for Microbial Research, Science for Life Laboratory (SciLifeLab), Department of Molecular Biology, Ume\u00e5 University, Ume\u00e5 90187, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/afac90582c374ab9b15102bc27516d89.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/afac90582c374ab9b15102bc27516d89"}}, "publications": [{"entity": "publication", "iuid": "a9cfff1aa2a24f22a98df7eee2f4eb5c", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/a9cfff1aa2a24f22a98df7eee2f4eb5c.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/a9cfff1aa2a24f22a98df7eee2f4eb5c"}}, "title": "Bacterial spore surface nanoenvironment requires a AAA+ ATPase to promote MurG function.", "authors": [{"family": "Delerue", "given": "Thomas", "initials": "T", "orcid": "0000-0002-8900-247X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/e98591b1cc0349f5bfd3aeaa9abfe5a6.json"}}, {"family": "Updegrove", "given": "Taylor B", "initials": "TB", "orcid": "0000-0002-9763-3618", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1f7584b3edb94db495422fd14557ee5f.json"}}, {"family": "Chareyre", "given": "Sylvia", "initials": "S"}, {"family": "Anantharaman", "given": "Vivek", "initials": "V", "orcid": "0000-0001-8395-0009", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/50872c7e2a114a5e9329134c0c0a203d.json"}}, {"family": "Gilmore", "given": "Michael C", "initials": "MC", "orcid": "0000-0002-6848-5134", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/afac90582c374ab9b15102bc27516d89.json"}}, {"family": "Jenkins", "given": "Lisa M", "initials": "LM", "orcid": "0000-0003-1245-1338", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/3dd3f6d782664134a47c5f2a67b774e3.json"}}, {"family": "Popham", "given": "David L", "initials": "DL", "orcid": "0000-0002-2614-143X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d7ccbe2816c54cfe9d729b794fcf6242.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}, {"family": "Aravind", "given": "L", "initials": "L", "orcid": "0000-0003-0771-253X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/2b3c1866cc2e407a9230dbff1e5609c8.json"}}, {"family": "Ramamurthi", "given": "Kumaran S", "initials": "KS"}], "type": "journal article", "published": "2024-10-22", "journal": {"title": "Proc. Natl. Acad. Sci. U.S.A.", "issn": "1091-6490", "volume": "121", "issue": "43", "pages": "e2414737121", "issn-l": "0027-8424"}, "abstract": "Bacillus subtilis spores are produced inside the cytosol of a mother cell. Spore surface assembly requires the SpoVK protein in the mother cell, but its function is unknown. Here, we report that SpoVK is a sporulation-specific, forespore-localized putative chaperone from a distinct higher-order clade of AAA+ ATPases that promotes the peptidoglycan glycosyltransferase activity of MurG during sporulation, even though MurG does not normally require activation during vegetative growth. MurG redeploys to the forespore surface during sporulation, where we show that the local pH is reduced and propose that this change in cytosolic nanoenvironment abrogates MurG function. Further, we show that SpoVK participates in a developmental checkpoint in which improper spore surface assembly mis-localizes SpoVK, which leads to sporulation arrest. The AAA+ ATPase clade containing SpoVK includes specialized chaperones involved in secretion, cell envelope biosynthesis, and carbohydrate metabolism, suggesting that such fine-tuning might be a widespread feature of different subcellular nanoenvironments.", "doi": "10.1073/pnas.2414737121", "pmid": "39405354", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11513918"}], "notes": [], "created": "2026-08-20T09:31:39.352Z", "modified": "2026-08-20T09:31:39.656Z"}, {"entity": "publication", "iuid": "dda09c0a9a3140d7b58c2557a6137522", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/dda09c0a9a3140d7b58c2557a6137522.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/dda09c0a9a3140d7b58c2557a6137522"}}, "title": "LD-transpeptidation is crucial for fitness and polar growth in Agrobacterium tumefaciens.", "authors": [{"family": "Aliashkevich", "given": "Alena", "initials": "A"}, {"family": "Guest", "given": "Thomas", "initials": "T", "orcid": "0000-0002-7868-0611", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0210aa68ff384d83947c28a5a65917e1.json"}}, {"family": "Alvarez", "given": "Laura", "initials": "L", "orcid": "0000-0003-2429-7542", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/329d8b1460fe44789dbef53ea0493294.json"}}, {"family": "Gilmore", "given": "Michael C", "initials": "MC", "orcid": "0000-0002-6848-5134", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/afac90582c374ab9b15102bc27516d89.json"}}, {"family": "Rea", "given": "Daniel", "initials": "D", "orcid": "0009-0009-6904-1031", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9f965bfb3ab44e82b84e6898fdf76ccf.json"}}, {"family": "Amstutz", "given": "Jennifer", "initials": "J"}, {"family": "Mateus", "given": "Andr\u00e9", "initials": "A", "orcid": "0000-0001-6870-0677", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ebf0d242aa894a66b60828456bbc22aa.json"}}, {"family": "Schiffthaler", "given": "Bastian", "initials": "B", "orcid": "0000-0002-9771-467X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0d53293c611f44dda99e9249b1614132.json"}}, {"family": "Ruiz", "given": "I\u00f1igo", "initials": "I"}, {"family": "Typas", "given": "Athanasios", "initials": "A", "orcid": "0000-0002-0797-9018", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d38ea7a531ad47cfa26df998f0e54dbe.json"}}, {"family": "Savitski", "given": "Mikhail M", "initials": "MM"}, {"family": "Brown", "given": "Pamela J B", "initials": "PJB", "orcid": "0000-0002-7558-7155", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/724518d7b8f24b438cd852bea2119e61.json"}}, {"family": "Cava", "given": "Felipe", "initials": "F", "orcid": "0000-0001-5995-718X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/bbcff12a06814d54afea533e125a1213.json"}}], "type": "journal article", "published": "2024-10-00", "journal": {"title": "PLoS Genet", "issn": "1553-7404", "volume": "20", "issue": "10", "pages": "e1011449", "issn-l": "1553-7390"}, "abstract": "Peptidoglycan (PG), a mesh-like structure which is the primary component of the bacterial cell wall, is crucial to maintain cell integrity and shape. While most bacteria rely on penicillin binding proteins (PBPs) for crosslinking, some species also employ LD-transpeptidases (LDTs). Unlike PBPs, the essentiality and biological functions of LDTs remain largely unclear. The Hyphomicrobiales order of the Alphaproteobacteria, known for their polar growth, have PG which is unusually rich in LD-crosslinks, suggesting that LDTs may play a more significant role in PG synthesis in these bacteria. Here, we investigated LDTs in the plant pathogen Agrobacterium tumefaciens and found that LD-transpeptidation, resulting from at least one of 14 putative LDTs present in this bacterium, is essential for its survival. Notably, a mutant lacking a distinctive group of 7 LDTs which are broadly conserved among the Hyphomicrobiales exhibited reduced LD-crosslinking and tethering of PG to outer membrane \u03b2-barrel proteins. Consequently, this mutant suffered severe fitness loss and cell shape rounding, underscoring the critical role played by these Hyphomicrobiales-specific LDTs in maintaining cell wall integrity and promoting elongation. Tn-sequencing screens further revealed non-redundant functions for A. tumefaciens LDTs. Specifically, Hyphomicrobiales-specific LDTs exhibited synthetic genetic interactions with division and cell cycle proteins, and a single LDT from another group. Additionally, our findings demonstrate that strains lacking all LDTs except one displayed distinctive phenotypic profiles and genetic interactions. Collectively, our work emphasizes the critical role of LD-crosslinking in A. tumefaciens cell wall integrity and growth and provides insights into the functional specialization of these crosslinking activities.", "doi": "10.1371/journal.pgen.1011449", "pmid": "39432536", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11527210"}, {"db": "pii", "key": "PGENETICS-D-24-00706"}], "notes": [], "created": "2026-08-20T12:43:54.428Z", "modified": "2026-08-20T12:43:54.645Z"}]}