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

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

doi:10.1016/S0092-8674(02)01248-5

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

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

422 Citations (Scopus)

Abstract

The Escherichia coli reIBE operon encodes a toxin-antitoxin pair, ReIE-ReIB. ReIB can reverse inhibition of protein synthesis by ReIE in vivo. We have found that although ReIE 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 ReIE is reversed with the help of tmRNA, and that ReIE plays a regulatory role in bacteria during adaptation to poor growth conditions.

Original language	English
Journal	Cell
Volume	112
Issue number	1
Pages (from-to)	131-140
Number of pages	10
ISSN	0092-8674
DOIs	https://doi.org/10.1016/S0092-8674(02)01248-5
Publication status	Published - 2003
Externally published	Yes

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10.1016/S0092-8674(02)01248-5

Cite this

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title = "The bacterial toxin RelE displays codon-specific cleavage of rnRNAs in the ribosomal A site",

abstract = "The Escherichia coli reIBE operon encodes a toxin-antitoxin pair, ReIE-ReIB. ReIB can reverse inhibition of protein synthesis by ReIE in vivo. We have found that although ReIE 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 ReIE is reversed with the help of tmRNA, and that ReIE plays a regulatory role in bacteria during adaptation to poor growth conditions.",

author = "K Pedersen and AV Zavialov and MY Pavlov and J Elf and K Gerdes and M Ehrenberg",

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T1 - The bacterial toxin RelE displays codon-specific cleavage of rnRNAs in the ribosomal A site

AU - Pedersen, K

AU - Zavialov, AV

AU - Pavlov, MY

AU - Elf, J

AU - Gerdes, K

AU - Ehrenberg, M

PY - 2003

Y1 - 2003

N2 - The Escherichia coli reIBE operon encodes a toxin-antitoxin pair, ReIE-ReIB. ReIB can reverse inhibition of protein synthesis by ReIE in vivo. We have found that although ReIE 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 ReIE is reversed with the help of tmRNA, and that ReIE plays a regulatory role in bacteria during adaptation to poor growth conditions.

AB - The Escherichia coli reIBE operon encodes a toxin-antitoxin pair, ReIE-ReIB. ReIB can reverse inhibition of protein synthesis by ReIE in vivo. We have found that although ReIE 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 ReIE is reversed with the help of tmRNA, and that ReIE plays a regulatory role in bacteria during adaptation to poor growth conditions.

U2 - 10.1016/S0092-8674(02)01248-5

DO - 10.1016/S0092-8674(02)01248-5

M3 - Journal article

SN - 0092-8674

VL - 112

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EP - 140

JO - Cell

JF - Cell

IS - 1

ER -