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NrnA is a 5′-3′ exonuclease that processes short RNA substrates in vivo and in vitro
Bacterial RNases process RNAs until only short oligomers (2–5 nucleotides) remain, which are then processed by one or more specialized enzymes until only nucleoside monophosphates remain. Oligoribonuclease (Orn) is an essential enzyme that acts in this capacity. However, many bacteria do not encode...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9757072/ https://www.ncbi.nlm.nih.gov/pubmed/36478094 http://dx.doi.org/10.1093/nar/gkac1091 |
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author | Weiss, Cordelia A Myers, Tanner M Wu, Chih Hao Jenkins, Conor Sondermann, Holger Lee, Vincent T Winkler, Wade C |
author_facet | Weiss, Cordelia A Myers, Tanner M Wu, Chih Hao Jenkins, Conor Sondermann, Holger Lee, Vincent T Winkler, Wade C |
author_sort | Weiss, Cordelia A |
collection | PubMed |
description | Bacterial RNases process RNAs until only short oligomers (2–5 nucleotides) remain, which are then processed by one or more specialized enzymes until only nucleoside monophosphates remain. Oligoribonuclease (Orn) is an essential enzyme that acts in this capacity. However, many bacteria do not encode for Orn and instead encode for NanoRNase A (NrnA). Yet, the catalytic mechanism, cellular roles and physiologically relevant substrates have not been fully resolved for NrnA proteins. We herein utilized a common set of reaction assays to directly compare substrate preferences exhibited by NrnA-like proteins from Bacillus subtilis, Enterococcus faecalis, Streptococcus pyogenes and Mycobacterium tuberculosis. While the M. tuberculosis protein specifically cleaved cyclic di-adenosine monophosphate, the B. subtilis, E. faecalis and S. pyogenes NrnA-like proteins uniformly exhibited striking preference for short RNAs between 2–4 nucleotides in length, all of which were processed from their 5′ terminus. Correspondingly, deletion of B. subtilis nrnA led to accumulation of RNAs between 2 and 4 nucleotides in length in cellular extracts. Together, these data suggest that many Firmicutes NrnA-like proteins are likely to resemble B. subtilis NrnA to act as a housekeeping enzyme for processing of RNAs between 2 and 4 nucleotides in length. |
format | Online Article Text |
id | pubmed-9757072 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-97570722022-12-19 NrnA is a 5′-3′ exonuclease that processes short RNA substrates in vivo and in vitro Weiss, Cordelia A Myers, Tanner M Wu, Chih Hao Jenkins, Conor Sondermann, Holger Lee, Vincent T Winkler, Wade C Nucleic Acids Res Nucleic Acid Enzymes Bacterial RNases process RNAs until only short oligomers (2–5 nucleotides) remain, which are then processed by one or more specialized enzymes until only nucleoside monophosphates remain. Oligoribonuclease (Orn) is an essential enzyme that acts in this capacity. However, many bacteria do not encode for Orn and instead encode for NanoRNase A (NrnA). Yet, the catalytic mechanism, cellular roles and physiologically relevant substrates have not been fully resolved for NrnA proteins. We herein utilized a common set of reaction assays to directly compare substrate preferences exhibited by NrnA-like proteins from Bacillus subtilis, Enterococcus faecalis, Streptococcus pyogenes and Mycobacterium tuberculosis. While the M. tuberculosis protein specifically cleaved cyclic di-adenosine monophosphate, the B. subtilis, E. faecalis and S. pyogenes NrnA-like proteins uniformly exhibited striking preference for short RNAs between 2–4 nucleotides in length, all of which were processed from their 5′ terminus. Correspondingly, deletion of B. subtilis nrnA led to accumulation of RNAs between 2 and 4 nucleotides in length in cellular extracts. Together, these data suggest that many Firmicutes NrnA-like proteins are likely to resemble B. subtilis NrnA to act as a housekeeping enzyme for processing of RNAs between 2 and 4 nucleotides in length. Oxford University Press 2022-12-07 /pmc/articles/PMC9757072/ /pubmed/36478094 http://dx.doi.org/10.1093/nar/gkac1091 Text en © The Author(s) 2022. 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 Weiss, Cordelia A Myers, Tanner M Wu, Chih Hao Jenkins, Conor Sondermann, Holger Lee, Vincent T Winkler, Wade C NrnA is a 5′-3′ exonuclease that processes short RNA substrates in vivo and in vitro |
title | NrnA is a 5′-3′ exonuclease that processes short RNA substrates in vivo and in vitro |
title_full | NrnA is a 5′-3′ exonuclease that processes short RNA substrates in vivo and in vitro |
title_fullStr | NrnA is a 5′-3′ exonuclease that processes short RNA substrates in vivo and in vitro |
title_full_unstemmed | NrnA is a 5′-3′ exonuclease that processes short RNA substrates in vivo and in vitro |
title_short | NrnA is a 5′-3′ exonuclease that processes short RNA substrates in vivo and in vitro |
title_sort | nrna is a 5′-3′ exonuclease that processes short rna substrates in vivo and in vitro |
topic | Nucleic Acid Enzymes |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9757072/ https://www.ncbi.nlm.nih.gov/pubmed/36478094 http://dx.doi.org/10.1093/nar/gkac1091 |
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