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The recognition of structured elements by a conserved groove distant from domains associated with catalysis is an essential determinant of RNase E

RNase E is an endoribonuclease found in many bacteria, including important human pathogens. Within Escherichia coli, it has been shown to have a major role in both the maturation of all classes of RNA involved in translation and the initiation of mRNA degradation. Thus, knowledge of the major determ...

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Detalles Bibliográficos
Autores principales: Clarke, Justin E, Sabharwal, Kiran, Kime, Louise, McDowall, Kenneth J
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9841416/
https://www.ncbi.nlm.nih.gov/pubmed/36594161
http://dx.doi.org/10.1093/nar/gkac1228
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author Clarke, Justin E
Sabharwal, Kiran
Kime, Louise
McDowall, Kenneth J
author_facet Clarke, Justin E
Sabharwal, Kiran
Kime, Louise
McDowall, Kenneth J
author_sort Clarke, Justin E
collection PubMed
description RNase E is an endoribonuclease found in many bacteria, including important human pathogens. Within Escherichia coli, it has been shown to have a major role in both the maturation of all classes of RNA involved in translation and the initiation of mRNA degradation. Thus, knowledge of the major determinants of RNase E cleavage is central to our understanding and manipulation of bacterial gene expression. We show here that the binding of RNase E to structured RNA elements is crucial for the processing of tRNA, can activate catalysis and may be important in mRNA degradation. The recognition of structured elements by RNase E is mediated by a recently discovered groove that is distant from the domains associated with catalysis. The functioning of this groove is shown here to be essential for E. coli cell viability and may represent a key point of evolutionary divergence from the paralogous RNase G family, which we show lack amino acid residues conserved within the RNA-binding groove of members of the RNase E family. Overall, this work provides new insights into the recognition and cleavage of RNA by RNase E and provides further understanding of the basis of RNase E essentiality in E. coli.
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spelling pubmed-98414162023-01-18 The recognition of structured elements by a conserved groove distant from domains associated with catalysis is an essential determinant of RNase E Clarke, Justin E Sabharwal, Kiran Kime, Louise McDowall, Kenneth J Nucleic Acids Res Nucleic Acid Enzymes RNase E is an endoribonuclease found in many bacteria, including important human pathogens. Within Escherichia coli, it has been shown to have a major role in both the maturation of all classes of RNA involved in translation and the initiation of mRNA degradation. Thus, knowledge of the major determinants of RNase E cleavage is central to our understanding and manipulation of bacterial gene expression. We show here that the binding of RNase E to structured RNA elements is crucial for the processing of tRNA, can activate catalysis and may be important in mRNA degradation. The recognition of structured elements by RNase E is mediated by a recently discovered groove that is distant from the domains associated with catalysis. The functioning of this groove is shown here to be essential for E. coli cell viability and may represent a key point of evolutionary divergence from the paralogous RNase G family, which we show lack amino acid residues conserved within the RNA-binding groove of members of the RNase E family. Overall, this work provides new insights into the recognition and cleavage of RNA by RNase E and provides further understanding of the basis of RNase E essentiality in E. coli. Oxford University Press 2023-01-03 /pmc/articles/PMC9841416/ /pubmed/36594161 http://dx.doi.org/10.1093/nar/gkac1228 Text en © The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Nucleic Acid Enzymes
Clarke, Justin E
Sabharwal, Kiran
Kime, Louise
McDowall, Kenneth J
The recognition of structured elements by a conserved groove distant from domains associated with catalysis is an essential determinant of RNase E
title The recognition of structured elements by a conserved groove distant from domains associated with catalysis is an essential determinant of RNase E
title_full The recognition of structured elements by a conserved groove distant from domains associated with catalysis is an essential determinant of RNase E
title_fullStr The recognition of structured elements by a conserved groove distant from domains associated with catalysis is an essential determinant of RNase E
title_full_unstemmed The recognition of structured elements by a conserved groove distant from domains associated with catalysis is an essential determinant of RNase E
title_short The recognition of structured elements by a conserved groove distant from domains associated with catalysis is an essential determinant of RNase E
title_sort recognition of structured elements by a conserved groove distant from domains associated with catalysis is an essential determinant of rnase e
topic Nucleic Acid Enzymes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9841416/
https://www.ncbi.nlm.nih.gov/pubmed/36594161
http://dx.doi.org/10.1093/nar/gkac1228
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