A Stress-Induced Bias in the Reading of the Genetic Code in <named-content content-type="genus-species">Escherichia coli</named-content>

ABSTRACT Escherichia coli mazEF is an extensively studied stress-induced toxin-antitoxin (TA) system. The toxin MazF is an endoribonuclease that cleaves RNAs at ACA sites. Thereby, under stress, the induced MazF generates a stress-induced translation machinery (STM), composed of MazF-processed mRNAs...

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Autores principales:	Adi Oron-Gottesman, Martina Sauert, Isabella Moll, Hanna Engelberg-Kulka
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2016
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/360ef97639a04efb8519a1cbc94e37b6
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spelling	oai:doaj.org-article:360ef97639a04efb8519a1cbc94e37b62021-11-15T15:50:15ZA Stress-Induced Bias in the Reading of the Genetic Code in <named-content content-type="genus-species">Escherichia coli</named-content>10.1128/mBio.01855-162150-7511https://doaj.org/article/360ef97639a04efb8519a1cbc94e37b62016-12-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.01855-16https://doaj.org/toc/2150-7511ABSTRACT Escherichia coli mazEF is an extensively studied stress-induced toxin-antitoxin (TA) system. The toxin MazF is an endoribonuclease that cleaves RNAs at ACA sites. Thereby, under stress, the induced MazF generates a stress-induced translation machinery (STM), composed of MazF-processed mRNAs and selective ribosomes that specifically translate the processed mRNAs. Here, we further characterized the STM system, finding that MazF cleaves only ACA sites located in the open reading frames of processed mRNAs, while out-of-frame ACAs are resistant. This in-frame ACA cleavage of MazF seems to depend on MazF binding to an extracellular-death-factor (EDF)-like element in ribosomal protein bS1 (bacterial S1), apparently causing MazF to be part of STM ribosomes. Furthermore, due to the in-frame MazF cleavage of ACAs under stress, a bias occurs in the reading of the genetic code causing the amino acid threonine to be encoded only by its synonym codon ACC, ACU, or ACG, instead of by ACA. IMPORTANCE The genetic code is a universal characteristic of all living organisms. It defines the set of rules by which nucleotide triplets specify which amino acid will be incorporated into a protein. Our results represent the first existing report on a stress-induced bias in the reading of the genetic code. We found that in E. coli, under stress, the amino acid threonine is encoded only by its synonym codon ACC, ACU, or ACG, instead of by ACA. This is because under stress, MazF generates a stress-induced translation machinery (STM) in which MazF cleaves in-frame ACA sites of the processed mRNAs.Adi Oron-GottesmanMartina SauertIsabella MollHanna Engelberg-KulkaAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 7, Iss 6 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 Adi Oron-Gottesman Martina Sauert Isabella Moll Hanna Engelberg-Kulka A Stress-Induced Bias in the Reading of the Genetic Code in <named-content content-type="genus-species">Escherichia coli</named-content>
description	ABSTRACT Escherichia coli mazEF is an extensively studied stress-induced toxin-antitoxin (TA) system. The toxin MazF is an endoribonuclease that cleaves RNAs at ACA sites. Thereby, under stress, the induced MazF generates a stress-induced translation machinery (STM), composed of MazF-processed mRNAs and selective ribosomes that specifically translate the processed mRNAs. Here, we further characterized the STM system, finding that MazF cleaves only ACA sites located in the open reading frames of processed mRNAs, while out-of-frame ACAs are resistant. This in-frame ACA cleavage of MazF seems to depend on MazF binding to an extracellular-death-factor (EDF)-like element in ribosomal protein bS1 (bacterial S1), apparently causing MazF to be part of STM ribosomes. Furthermore, due to the in-frame MazF cleavage of ACAs under stress, a bias occurs in the reading of the genetic code causing the amino acid threonine to be encoded only by its synonym codon ACC, ACU, or ACG, instead of by ACA. IMPORTANCE The genetic code is a universal characteristic of all living organisms. It defines the set of rules by which nucleotide triplets specify which amino acid will be incorporated into a protein. Our results represent the first existing report on a stress-induced bias in the reading of the genetic code. We found that in E. coli, under stress, the amino acid threonine is encoded only by its synonym codon ACC, ACU, or ACG, instead of by ACA. This is because under stress, MazF generates a stress-induced translation machinery (STM) in which MazF cleaves in-frame ACA sites of the processed mRNAs.
format	article
author	Adi Oron-Gottesman Martina Sauert Isabella Moll Hanna Engelberg-Kulka
author_facet	Adi Oron-Gottesman Martina Sauert Isabella Moll Hanna Engelberg-Kulka
author_sort	Adi Oron-Gottesman
title	A Stress-Induced Bias in the Reading of the Genetic Code in <named-content content-type="genus-species">Escherichia coli</named-content>
title_short	A Stress-Induced Bias in the Reading of the Genetic Code in <named-content content-type="genus-species">Escherichia coli</named-content>
title_full	A Stress-Induced Bias in the Reading of the Genetic Code in <named-content content-type="genus-species">Escherichia coli</named-content>
title_fullStr	A Stress-Induced Bias in the Reading of the Genetic Code in <named-content content-type="genus-species">Escherichia coli</named-content>
title_full_unstemmed	A Stress-Induced Bias in the Reading of the Genetic Code in <named-content content-type="genus-species">Escherichia coli</named-content>
title_sort	stress-induced bias in the reading of the genetic code in <named-content content-type="genus-species">escherichia coli</named-content>
publisher	American Society for Microbiology
publishDate	2016
url	https://doaj.org/article/360ef97639a04efb8519a1cbc94e37b6
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A Stress-Induced Bias in the Reading of the Genetic Code in <named-content content-type="genus-species">Escherichia coli</named-content>

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