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A hyperpromiscuous ...
A hyperpromiscuous antitoxin protein domain for the neutralization of diverse toxin domains
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- Kurata, Tatsuaki (författare)
- Lund University,Lunds universitet,Molekylär enzymologi,Forskargrupper vid Lunds universitet,Molecular Enzymology,Lund University Research Groups
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- Saha, Chayan Kumar (författare)
- Umeå University,Lund University,Lunds universitet,Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Department of Experimental Medicine, University of Lund, Lund, Sweden,Proteinevolution,Forskargrupper vid Lunds universitet,Protein Evolution,Lund University Research Groups
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- Buttress, Jessica A. (författare)
- University of Newcastle
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- Mets, Toomas (författare)
- University of Tartu
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- Brodiazhenko, Tetiana (författare)
- University of Tartu
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- Turnbull, Kathryn J. (författare)
- Copenhagen University Hospital
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- Awoyomi, Ololade F. (författare)
- Umeå University,Umeå universitet,Institutionen för medicinsk kemi och biofysik
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- Oliveira, Sofia Raquel Alves (författare)
- University of Tartu
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- Jimmy, Steffi (författare)
- German Electron Synchrotron (DESY)
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- Ernits, Karin (författare)
- Umeå University,Umeå universitet,Kemiska institutionen
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- Delannoy, Maxence (författare)
- Université Nice Sophia Antipolis
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- Persson, Karina (författare)
- Umeå University,Umeå universitet,Kemiska institutionen
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- Tenson, Tanel (författare)
- Tartu University Library
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- Strahl, Henrik (författare)
- University of Newcastle
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- Hauryliuk, Vasili, 1980- (författare)
- Umeå University,Lund University,Lunds universitet,Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Molekylär Infektionsmedicin, Sverige (MIMS),Department of Experimental Medicine, University of Lund, Lund, Sweden; University of Tartu, Institute of Technology, Tartu, Estonia,Molekylär enzymologi,Forskargrupper vid Lunds universitet,Molecular Enzymology,Lund University Research Groups
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- Atkinson, Gemma C. (författare)
- Umeå University,Lund University,Lunds universitet,Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Department of Experimental Medicine, University of Lund, Lund, Sweden,Proteinevolution,Forskargrupper vid Lunds universitet,Protein Evolution,Lund University Research Groups
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(creator_code:org_t)
- 2022-02-04
- 2022
- Engelska.
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Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 119:6
- Relaterad länk:
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https://doi.org/10.1...
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https://umu.diva-por... (primary) (Raw object)
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https://www.pnas.org...
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http://dx.doi.org/10... (free)
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://lup.lub.lu.s...
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Abstract
Ämnesord
Stäng
- Toxin–antitoxin (TA) gene pairs are ubiquitous in microbial chromosomal genomes and plasmids as well as temperate bacteriophages. They act as regulatory switches, with the toxin limiting the growth of bacteria and archaea by compromising diverse essential cellular targets and the antitoxin counteracting the toxic effect. To uncover previously uncharted TA diversity across microbes and bacteriophages, we analyzed the conservation of genomic neighborhoods using our computational tool FlaGs (for flanking genes), which allows high-throughput detection of TA-like operons. Focusing on the widespread but poorly experimentally characterized antitoxin domain DUF4065, our in silico analyses indicated that DUF4065-containing proteins serve as broadly distributed antitoxin components in putative TA-like operons with dozens of different toxic domains with multiple different folds. Given the versatility of DUF4065, we have named the domain Panacea (and proteins containing the domain, PanA) after the Greek goddess of universal remedy. We have experimentally validated nine PanA-neutralized TA pairs. While the majority of validated PanA-neutralized toxins act as translation inhibitors or membrane disruptors, a putative nucleotide cyclase toxin from a Burkholderia prophage compromises transcription and translation as well as inducing RelA-dependent accumulation of the nucleotide alarmone (p)ppGpp. We find that Panacea-containing antitoxins form a complex with their diverse cognate toxins, characteristic of the direct neutralization mechanisms employed by Type II TA systems. Finally, through directed evolution, we have selected PanA variants that can neutralize noncognate TA toxins, thus experimentally demonstrating the evolutionary plasticity of this hyperpromiscuous antitoxin domain.
Ämnesord
- NATURVETENSKAP -- Biologi -- Mikrobiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Microbiology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
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Kurata, Tatsuaki
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Saha, Chayan Kum ...
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Buttress, Jessic ...
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Mets, Toomas
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Brodiazhenko, Te ...
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Turnbull, Kathry ...
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visa fler...
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Awoyomi, Ololade ...
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Oliveira, Sofia ...
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Jimmy, Steffi
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Ernits, Karin
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Delannoy, Maxenc ...
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Persson, Karina
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Tenson, Tanel
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Strahl, Henrik
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Hauryliuk, Vasil ...
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Atkinson, Gemma ...
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visa färre...
- Om ämnet
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- NATURVETENSKAP
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NATURVETENSKAP
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och Biologi
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och Mikrobiologi
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- NATURVETENSKAP
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NATURVETENSKAP
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och Biologi
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och Biokemi och mole ...
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Proceedings of t ...
- Av lärosätet
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Umeå universitet
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Lunds universitet