RnlB Antitoxin of the Escherichia Coli RnlA-RnlB Toxin-Antitoxin Module Requires RNase HI for Inhibition of RnlA Toxin Activity

Overview

Journal Toxins (Basel)

Publisher MDPI

Specialty Toxicology

Date 2017 Jan 14

PMID 28085056

Citations 6

Authors

Kenta Naka

Dan Qi

Tetsuro Yonesaki

Yuichi Otsuka

Affiliations

Soon will be listed here.

Abstract

The RnlA-RnlB toxin-antitoxin system is related to the anti-phage mechanism. Under normal growth conditions, an RnlA toxin with endoribonuclease activity is inhibited by binding of its cognate RnlB antitoxin. After bacteriophage T4 infection, RnlA is activated by the disappearance of RnlB, resulting in the rapid degradation of T4 mRNAs and consequently no T4 propagation when T4 encoding a phage antitoxin against RnlA is defective. Intriguingly, RNase HI, which plays a key role in DNA replication, is required for the activation of RnlA and stimulates the RNA cleavage activity of RnlA. Here, we report an additional role of RNase HI in the regulation of RnlA-RnlB system. Both RNase HI and RnlB are associated with NRD (one of three domains of RnlA). The interaction between RnlB and NRD depends on RNase HI. Exogenous expression of RnlA in wild-type cells has no effect on cell growth because of endogenous RnlB and this inhibition of RnlA toxicity requires RNase HI and NRD. These results suggest that RNase HI recruits RnlB to RnlA through NRD for inhibiting RnlA toxicity and thus plays two contrary roles in the regulation of RnlA-RnlB system.

Citing Articles

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

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Shutoff of host transcription triggers a toxin-antitoxin system to cleave phage RNA and abort infection.

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