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BMB Reports

Substrate specificity of bacterial endoribonuclease toxins

  • 작성자

    관리자
  • 작성일자

    2020-11-23
  • 조회수

    224
2018-present Associate Professor, Department of Life Sciences, Korea University
2013-2018 Assistant & Associate Professor, Department of Genetic Engineering, Kyung Hee University
2010-2013 Research Specialist, Yale University, USA
2004-2010 Research Associate, Washington University in St. Louis, USA

Substrate specificity of bacterial endoribonuclease toxins

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 toxin’s activity is antagonized by antitoxin proteins or RNAs during active translation. In response to a variety of cellular stresses, the endoribonuclease toxins are 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, contributing to various biological phenomena such as antibiotic tolerance and persister formation. Given that substrate specificity of each ribonuclease toxin is determined by its structure and the composition of active site residues, here we summarize the biology, structure, and substrate specificity of the updated bacterial endoribonuclease toxins

https://pubmed.ncbi.nlm.nih.gov/33148377/
BMB Rep 2020 Nov 4;5175. Online ahead of print