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 Citationer (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.

Originalsprog	Engelsk
Tidsskrift	Cell
Vol/bind	112
Udgave nummer	1
Sider (fra-til)	131-140
Antal sider	10
ISSN	0092-8674
DOI	https://doi.org/10.1016/S0092-8674(02)01248-5
Status	Udgivet - 2003
Udgivet eksternt	Ja

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10.1016/S0092-8674(02)01248-5

Citationsformater

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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",

year = "2003",

doi = "10.1016/S0092-8674(02)01248-5",

language = "English",

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pages = "131--140",

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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

SP - 131

EP - 140

JO - Cell

JF - Cell

IS - 1

ER -