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Bacterial cell surface nanoenvironment requires a specialized chaperone to activate a peptidoglycan biosynthetic enzyme
Open accessPreprint — published as 10.1073/pnas.2414737121
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 dedicated chaperone from a distinct higher-order clade of AAA+ ATPases that activates the peptidoglycan glycosyltransferase MurG during sporulation, even though MurG does not normally require activation by a chaperone during vegetative growth. MurG redeploys to the spore surface during sporulation, where we show that the local pH is reduced and propose that this change in cytosolic nanoenvironment necessitates a specific chaperone for proper MurG function. Further, we show that SpoVK participates in a developmental checkpoint in which improper spore surface assembly inactivates SpoVK, which leads to sporulation arrest. The AAA+ ATPase clade containing SpoVK includes other dedicated chaperones involved in secretion, cell-envelope biosynthesis, and carbohydrate metabolism, suggesting that such fine-tuning might be a widespread feature of different subcellular nanoenvironments.
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Metadata
- Authors
- Delerue, T., Chareyre, S., Anantharaman, V., Gilmore, M. C., Popham, D. L., Cava, F., Aravind, L., & Ramamurthi, K. S.
- Affiliations
- National Institutes of Health (US)
- Science for Life Laboratory (SE)
- Virginia Tech (US)
- Corresponding author
- Delerue, Thomas
- Chareyre, Sylvia
- Ramamurthi, Kumaran S.
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- openRxiv
- Published
- 2023-10-06
- Volume
- 121
- Issue
- 43
- Pages
- e2414737121-e2414737121
- ISSN
- 0027-8424 (ISSN-L)
- PMC
- PMC11513918
- OpenAlex
- W4403419211
- Cited by
- 4
- References
- 1
- Citations by year
- 2026: 3 · 2025: 1
- FWCI
- 1.06
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (submittedVersion, public-domain)
- DiVA at Umeå University (Umeå University) (submittedVersion, other-oa)
- Funders
- Kemper Foundation
- Kempe Foundation
- Knut och Alice Wallenbergs Stiftelse
- Vetenskapsrådet
- Umeå Universitet
- National Institutes of Health
- National Cancer Institute
- National Institute of General Medical Sciences (R01GM138630)
- U.S. National Library of Medicine
- NHLBI Division of Intramural Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- AAA+ ATPase, MurG, forespore, sporulation, intracellular pH, molecular chaperones, developmental checkpoints, cell envelope biosynthesis
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