Invited Mini Review Substrate specificity of bacterial endoribonuclease toxins

Yoontak Han, Eun Jin Lee

Research output: Contribution to journalArticlepeer-review

Abstract

Bacterial endoribonuclease toxins belong to a protein family that inhibits bacterial growth by degrading mRNA or rRNA sequences. The toxin genes are organized in pairs with its cognate antitoxins in the chromosome and thus the activities of the toxins are antagonized by antitoxin proteins or RNAs during active translation. In response to a variety of cellular stresses, the endoribonuclease toxins appear to be released from antitoxin molecules via proteolytic cleavage of antitoxin proteins or preferential degradation of antitoxin RNAs and cleave a diverse range of mRNA or rRNA sequences in a sequence-specific or codon-specific manner, resulting in various biological phenomena such as antibiotic tolerance and persister cell formation. Given that substrate specificity of each endoribonuclease toxin is determined by its structure and the composition of active site residues, we summarize the biology, structure, and substrate specificity of the updated bacterial endoribonuclease toxins. [BMB Reports 2020; 53(12): 611-621]

Original languageEnglish
Pages (from-to)611-621
Number of pages11
JournalBMB reports
Volume53
Issue number12
DOIs
Publication statusPublished - 2020

Keywords

  • Endoribonuclease
  • Persister cells
  • Recognition sequence
  • Ribosome
  • Toxin-antitoxin system

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Fingerprint

Dive into the research topics of 'Invited Mini Review Substrate specificity of bacterial endoribonuclease toxins'. Together they form a unique fingerprint.

Cite this