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About:
Functional plasticity of antibacterial EndoU toxins
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wasabi.inria.fr
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Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
has title
Functional plasticity of antibacterial EndoU toxins
Creator
Joachimiak, Andrzej
Koskiniemi, Sanna
Michalska, Karolina
Hayes, Christopher
Eschenfeldt, William
Goulding, Celia
Stols, Lucy
Willett, Julia
Dinh, ‡
Jones, Allison
Low, David
Nguyen, Josephine
Nhan, Quan
Source
Medline; PMC
abstract
Bacteria use several different secretion systems to deliver toxic EndoU ribonucleases into neighboring cells. Here, we present the first structure of a prokaryotic EndoU toxin in complex with its cognate immunity protein. The contact-dependent growth inhibition toxin CdiA-CT(STECO31) from Escherichia coli STEC_O31 adopts the eukaryotic EndoU fold and shares greatest structural homology with the nuclease domain of coronavirus Nsp15. The toxin contains a canonical His-His-Lys catalytic triad in the same arrangement as eukaryotic EndoU domains, but lacks the uridylate-specific ribonuclease activity that characterizes the superfamily. Comparative sequence analysis indicates that bacterial EndoU domains segregate into at least three major clades based on structural variations in the N-terminal subdomain. Representative EndoU nucleases from clades I and II degrade tRNA molecules with little specificity. In contrast, CdiA-CT(STECO31) and other clade III toxins are specific anticodon nucleases that cleave tRNA(Glu) between nucleotides C37 and m(2)A38. These findings suggest that the EndoU fold is a versatile scaffold for the evolution of novel substrate specificities. Such functional plasticity may account for the widespread use of EndoU effectors by diverse inter-bacterial toxin delivery systems.
has issue date
2018-08-01
(
xsd:dateTime
)
bibo:doi
10.1111/mmi.14007
bibo:pmid
29923643
has license
bronze-oa
sha1sum (hex)
776c56df617a70429e9a2a23b8926ed854af43d0
schema:url
https://doi.org/10.1111/mmi.14007
resource representing a document's title
Functional plasticity of antibacterial EndoU toxins
has PubMed Central identifier
PMC6173971
has PubMed identifier
29923643
schema:publication
Molecular Microbiology
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covid:776c56df617a70429e9a2a23b8926ed854af43d0#body_text
is
schema:about
of
named entity 'scaffold'
named entity 'nucleases'
named entity 'anticodon'
named entity 'These'
named entity 'protein'
named entity 'Glu'
named entity 'shares'
named entity 'complex'
named entity 'evolution'
named entity 'subdomain'
named entity 'structure'
named entity 'deliver'
named entity 'clades'
named entity 'clades'
named entity 'toxin'
named entity 'nucleotides'
named entity 'toxin'
named entity 'molecules'
named entity 'antibacterial'
named entity 'Comparative sequence analysis'
named entity 'toxin'
named entity 'toxin'
named entity 'clades'
named entity 'clade'
named entity 'clades'
named entity 'structural variations'
named entity 'catalytic triad'
named entity 'nucleases'
named entity 'protein'
named entity 'prokaryotic'
named entity 'plasmid'
named entity 'nuclease'
named entity 'fusion protein'
named entity 'Bacillus cereus'
named entity 'RNA extraction'
named entity 'selenomethionine'
named entity 'catalytic triad'
named entity 'RNase'
named entity 'millimolar'
named entity 'Clade'
named entity '3 10 helix'
named entity 'Gels'
named entity 'protein toxins'
named entity 'co-cultures'
named entity 'toxin'
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named entity 'catalytic mechanism'
named entity 'tRNA'
named entity 'secretion systems'
named entity '2-mercaptoethanol'
named entity 'phosphorimaging'
named entity 'CdiI'
named entity 'wildtype'
named entity 'toxin'
named entity 'Tris-HCl'
named entity 'denoted by a prime'
named entity 'Nuclease'
named entity 'C-termini'
named entity 'NaCl'
named entity 'C-terminal'
named entity 'vitamins'
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named entity 'RNAs'
named entity 'titration'
named entity 'clones'
named entity 'E. coli'
named entity 'plasmid'
named entity 'anticodon'
named entity 'active site'
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