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Substrate-dependent effects of quaternary structure on RNase E activity
RNase E is an essential, multifunctional ribonuclease encoded in E. coli by the rne gene. Structural analysis indicates that the ribonucleolytic activity of this enzyme is conferred by rne-encoded polypeptide chains that (1) dimerize to form a catalytic site at the protein-protein interface, and (2)...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7849360/ https://www.ncbi.nlm.nih.gov/pubmed/33446571 http://dx.doi.org/10.1101/gad.335828.119 |
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author | Moore, Christopher J. Go, Hayoung Shin, Eunkyoung Ha, Hye-Jeong Song, Saemee Ha, Nam-Chul Kim, Yong-Hak Cohen, Stanley N. Lee, Kangseok |
author_facet | Moore, Christopher J. Go, Hayoung Shin, Eunkyoung Ha, Hye-Jeong Song, Saemee Ha, Nam-Chul Kim, Yong-Hak Cohen, Stanley N. Lee, Kangseok |
author_sort | Moore, Christopher J. |
collection | PubMed |
description | RNase E is an essential, multifunctional ribonuclease encoded in E. coli by the rne gene. Structural analysis indicates that the ribonucleolytic activity of this enzyme is conferred by rne-encoded polypeptide chains that (1) dimerize to form a catalytic site at the protein-protein interface, and (2) multimerize further to generate a tetrameric quaternary structure consisting of two dimerized Rne-peptide chains. We identify here a mutation in the Rne protein's catalytic region (E429G), as well as a bacterial cell wall peptidoglycan hydrolase (Amidase C [AmiC]), that selectively affect the specific activity of the RNase E enzyme on long RNA substrates, but not on short synthetic oligonucleotides, by enhancing enzyme multimerization. Unlike the increase in specific activity that accompanies concentration-induced multimerization, enhanced multimerization associated with either the E429G mutation or interaction of the Rne protein with AmiC is independent of the substrate's 5′ terminus phosphorylation state. Our findings reveal a previously unsuspected substrate length-dependent regulatory role for RNase E quaternary structure and identify cis-acting and trans-acting factors that mediate such regulation. |
format | Online Article Text |
id | pubmed-7849360 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-78493602021-08-01 Substrate-dependent effects of quaternary structure on RNase E activity Moore, Christopher J. Go, Hayoung Shin, Eunkyoung Ha, Hye-Jeong Song, Saemee Ha, Nam-Chul Kim, Yong-Hak Cohen, Stanley N. Lee, Kangseok Genes Dev Research Paper RNase E is an essential, multifunctional ribonuclease encoded in E. coli by the rne gene. Structural analysis indicates that the ribonucleolytic activity of this enzyme is conferred by rne-encoded polypeptide chains that (1) dimerize to form a catalytic site at the protein-protein interface, and (2) multimerize further to generate a tetrameric quaternary structure consisting of two dimerized Rne-peptide chains. We identify here a mutation in the Rne protein's catalytic region (E429G), as well as a bacterial cell wall peptidoglycan hydrolase (Amidase C [AmiC]), that selectively affect the specific activity of the RNase E enzyme on long RNA substrates, but not on short synthetic oligonucleotides, by enhancing enzyme multimerization. Unlike the increase in specific activity that accompanies concentration-induced multimerization, enhanced multimerization associated with either the E429G mutation or interaction of the Rne protein with AmiC is independent of the substrate's 5′ terminus phosphorylation state. Our findings reveal a previously unsuspected substrate length-dependent regulatory role for RNase E quaternary structure and identify cis-acting and trans-acting factors that mediate such regulation. Cold Spring Harbor Laboratory Press 2021-02-01 /pmc/articles/PMC7849360/ /pubmed/33446571 http://dx.doi.org/10.1101/gad.335828.119 Text en © 2021 Moore et al.; Published by Cold Spring Harbor Laboratory Press http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/. |
spellingShingle | Research Paper Moore, Christopher J. Go, Hayoung Shin, Eunkyoung Ha, Hye-Jeong Song, Saemee Ha, Nam-Chul Kim, Yong-Hak Cohen, Stanley N. Lee, Kangseok Substrate-dependent effects of quaternary structure on RNase E activity |
title | Substrate-dependent effects of quaternary structure on RNase E activity |
title_full | Substrate-dependent effects of quaternary structure on RNase E activity |
title_fullStr | Substrate-dependent effects of quaternary structure on RNase E activity |
title_full_unstemmed | Substrate-dependent effects of quaternary structure on RNase E activity |
title_short | Substrate-dependent effects of quaternary structure on RNase E activity |
title_sort | substrate-dependent effects of quaternary structure on rnase e activity |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7849360/ https://www.ncbi.nlm.nih.gov/pubmed/33446571 http://dx.doi.org/10.1101/gad.335828.119 |
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