The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site.

Abstract:

:The Escherichia coli relBE operon encodes a toxin-antitoxin pair, RelE-RelB. RelB can reverse inhibition of protein synthesis by RelE in vivo. We have found that although RelE does not degrade free RNA, it cleaves mRNA in the ribosomal A site with high codon specificity. Among stop codons UAG is cleaved with fast, UAA intermediate and UGA slow rate, while UCG and CAG are cleaved most rapidly among sense codons. We suggest that inhibition of protein synthesis by RelE is reversed with the help of tmRNA, and that RelE plays a regulatory role in bacteria during adaptation to poor growth conditions.

journal_name

Cell

journal_title

Cell

authors

Pedersen K,Zavialov AV,Pavlov MY,Elf J,Gerdes K,Ehrenberg M

doi

10.1016/s0092-8674(02)01248-5

subject

Has Abstract

pub_date

2003-01-10 00:00:00

pages

131-40

issue

1

eissn

0092-8674

issn

1097-4172

pii

S0092867402012485

journal_volume

112

pub_type

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