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Article

Alternative dimerization is required for activity and inhibition of the HEPN ribonuclease RnlA.

Nucleic acids research - 9 Jul 2021

Garcia-Rodriguez Gabriela, Charlier Daniel, Wilmaerts Dorien, Michiels Jan, Loris Remy

Abstract excerpt

The rnlAB toxin-antitoxin operon from Escherichia coli functions as an anti-phage defense system. RnlA was identified as a member of the HEPN (Higher Eukaryotes and Prokaryotes Nucleotide-binding domain) superfamily of ribonucleases. The activity of the toxin RnlA requires tight regulation by the antitoxin RnlB, the mechanism of which remains unknown. Here we show that RnlA exists in an equilibrium between two...

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Identifiers

PMID: 34139012
DOI: 10.1093/nar/gkab513
PMCID: PMC8266594

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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