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A new family of bacterial ribosome hibernation factors |
Tartalom: | https://real.mtak.hu/214379/ |
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Archívum: | REAL |
Gyűjtemény: |
Status = Published
Subject = Q Science / természettudomány: QR Microbiology / mikrobiológia: QR180 Immunology / immunológia Subject = Q Science / természettudomány: QR Microbiology / mikrobiológia Subject = Q Science / természettudomány: QH Natural history / természetrajz: QH301 Biology / biológia Subject = Q Science / természettudomány: QH Natural history / természetrajz: QH301 Biology / biológia: QH3015 Molecular biology / molekuláris biológia Type = Article |
Cím: |
A new family of bacterial ribosome hibernation factors
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Létrehozó: |
Helena-Bueno, Karla
Rybak, Mariia Yu.
Ekemezie, Chinenye L.
Sullivan, Rudi
Brown, Charlotte R.
Dingwall, Charlotte
Basle, Arnaud
Schneider, Claudia
Connolly, James P. R.
Blaza, James N.
Csörgő, Bálint
Moynihan, Patrick J.
Gagnon, Matthieu G.
Hill, Chris H.
Melnikov, Sergey V.
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Dátum: |
2024
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Téma: |
QH301 Biology / biológia
QH3015 Molecular biology / molekuláris biológia
QR Microbiology / mikrobiológia
QR180 Immunology / immunológia
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Tartalmi leírás: |
To conserve energy during starvation and stress, many organisms use hibernation factor proteins to inhibit protein synthesis and protect their ribosomes from damage1,2. In bacteria, two families of hibernation factors have been described, but the low conservation of these proteins and the huge diversity of species, habitats and environmental stressors have confounded their discovery3-6. Here, by combining cryogenic electron microscopy, genetics and biochemistry, we identify Balon, a new hibernation factor in the cold-adapted bacterium Psychrobacter urativorans. We show that Balon is a distant homologue of the archaeo-eukaryotic translation factor aeRF1 and is found in 20% of representative bacteria. During cold shock or stationary phase, Balon occupies the ribosomal A site in both vacant and actively translating ribosomes in complex with EF-Tu, highlighting an unexpected role for EF-Tu in the cellular stress response. Unlike typical A-site substrates, Balon binds to ribosomes in an mRNA-independent manner, initiating a new mode of ribosome hibernation that can commence while ribosomes are still engaged in protein synthesis. Our work suggests that Balon-EF-Tu-regulated ribosome hibernation is a ubiquitous bacterial stress-response mechanism, and we demonstrate that putative Balon homologues in Mycobacteria bind to ribosomes in a similar fashion. This finding calls for a revision of the current model of ribosome hibernation inferred from common model organisms and holds numerous implications for how we understand and study ribosome hibernation. A study identifies a new bacterial ribosome hibernation factor, Balon, and describes its association with EF-Tu and its initiation of mRNA-independent hibernation during protein synthesis.
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Nyelv: |
angol
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Típus: |
Article
PeerReviewed
info:eu-repo/semantics/article
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Formátum: |
text
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Azonosító: |
Helena-Bueno, Karla and Rybak, Mariia Yu. and Ekemezie, Chinenye L. and Sullivan, Rudi and Brown, Charlotte R. and Dingwall, Charlotte and Basle, Arnaud and Schneider, Claudia and Connolly, James P. R. and Blaza, James N. and Csörgő, Bálint and Moynihan, Patrick J. and Gagnon, Matthieu G. and Hill, Chris H. and Melnikov, Sergey V. (2024) A new family of bacterial ribosome hibernation factors. NATURE, 626 (8001). pp. 1125-1132. ISSN 0028-0836
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Kapcsolat: |
MTMT:34782533 10.1038/s41586-024-07041-8
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Létrehozó: |
cc_by
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