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Bacteria use processing body condensates to attenuate host translation during infection
Open accessPreprint — published as 10.1126/sciadv.aec4477
Abstract
Pathogens employ sophisticated strategies to modulate host protein homeostasis by targeting proteolytic pathways, but their impact on protein synthesis remains elusive. We report that pathogenic bacteria Pseudomonas syringae ( Pst ) targets ribonucleoprotein condensates, known as processing bodies (P-bodies), to attenuate host translation through two effectors with liquid-like properties. We uncovered a previously unknown link that Pst -mediated repression of the ER stress response is required for P-body assembly. Furthermore, we identify a novel intersection between P-bodies and autophagy, demonstrating that autophagic clearance of P-bodies is crucial for maintaining the balance between translationally active and inactive mRNAs. Altogether, our discoveries provide novel insights on how host translation is attenuated by bacteria to dampen plant immunity and uncover unknown connections between ER stress responses and autophagy with P-body dynamics.
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Metadata
- Authors
- González-Fuente, M., Schulz, N., Abdrakhmanov, A., Izzati, G., Zhu, S., Langin, G., Gouguet, P., Franz-Wachtel, M., Macek, B., Hafrén, A., Dagdas, Y., & Üstün, S.
- Affiliations
- Faculty of Biology and Biotechnology, Ruhr-University Bochum; Bochum, 44780, Germany
- Ruhr University Bochum (DE)
- University of Vienna (AT)
- University of Tübingen (DE)
- Proteome Center Tübingen, Interfaculty Institute for Cell Biology, University of Tübingen; Tübingen, 72076, Germany
- Swedish University of Agricultural Sciences (SE)
- Gregor Mendel Institute of Molecular Plant Biology (AT)
- ORCID
- Venue
- Science Advances
- Publisher
- openRxiv
- Published
- 2025-01-14
- Volume
- 12
- Issue
- 17
- Pages
- eaec4477-eaec4477
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC13108548
- OpenAlex
- W7155491829
- Cited by
- 4
- References
- 1
- Citations by year
- 2026: 1 · 2025: 3
- FWCI
- 3.70
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Science Advances (publishedVersion, cc-by-nc)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Funders
- European Commission
- Deutsche Forschungsgemeinschaft (INST 37/965‐1 FUGG, UE188/2‐1, INST 213/1180-1 FUGG, DFG INST 37/819-1 FUGG, GO 3479/1-1)
- University of Toronto
- Université de Strasbourg
- Vetenskapsrådet (2022-03846)
- Boehringer Ingelheim Stiftung
- European Research Council (948996 DIVERSIPHAGY)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Pathogenic Bacteria Studies
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant-Microbe Interactions and Immunity
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- Pseudomonas syringae, P-bodies, ribonucleoprotein condensates, bacterial effector proteins, endoplasmic reticulum stress response, autophagy, plant immunity, plant-pathogen interaction, mRNA degradation
- MeSH terms
- Biomolecular Condensates, Autophagy, Plant Diseases, Ribonucleoproteins, RNA, Messenger, Protein Biosynthesis, Arabidopsis, Pseudomonas syringae, Host-Pathogen Interactions, Plant Immunity, Endoplasmic Reticulum Stress
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