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Examining the Protein Interactome and Subcellular Localization of RNase J2 Complexes in Streptococcus mutans

Regulated RNA turnover is vital for the control of gene expression in all cellular life. In Escherichia coli, this process is largely controlled by a stable degradosome complex containing RNase E and a variety of additional enzymes. In the Firmicutes phylum, species lack RNase E and often encode the...

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Autores principales: Mu, Rong, Shinde, Pushkar, Zou, Zhengzhong, Kreth, Jens, Merritt, Justin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6759994/
https://www.ncbi.nlm.nih.gov/pubmed/31620106
http://dx.doi.org/10.3389/fmicb.2019.02150
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author Mu, Rong
Shinde, Pushkar
Zou, Zhengzhong
Kreth, Jens
Merritt, Justin
author_facet Mu, Rong
Shinde, Pushkar
Zou, Zhengzhong
Kreth, Jens
Merritt, Justin
author_sort Mu, Rong
collection PubMed
description Regulated RNA turnover is vital for the control of gene expression in all cellular life. In Escherichia coli, this process is largely controlled by a stable degradosome complex containing RNase E and a variety of additional enzymes. In the Firmicutes phylum, species lack RNase E and often encode the paralogous enzymes RNase J1 and RNase J2. Unlike RNase J1, surprisingly little is known about the regulatory function and protein interactions of RNase J2, despite being a central pleiotropic regulator for the streptococci and other closely related organisms. Using crosslink coimmunoprecipitation in Streptococcus mutans, we have identified the major proteins found within RNase J2 protein complexes located in the cytoplasm and at the cell membrane. In both subcellular fractions, RNase J2 exhibited the most robust interactions with RNase J1, while additional transient and/or weaker “degradosome-like” interactions were also detected. In addition, RNase J2 exhibits multiple novel interactions that have not been previously reported for any RNase J proteins, some of which were highly biased for either the cytoplasmic or membrane fractions. We also determined that the RNase J2 C-terminal domain (CTD) encodes a structure that is likely conserved among RNase J enzymes and may have an analogous function to the C-terminal portion of RNase E. While we did observe a number of parallels between the RNase J2 interactome and the E. coli degradosome paradigm, our results suggest that S. mutans degradosomes are either unlikely to exist or are quite distinct from those of E. coli.
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spelling pubmed-67599942019-10-16 Examining the Protein Interactome and Subcellular Localization of RNase J2 Complexes in Streptococcus mutans Mu, Rong Shinde, Pushkar Zou, Zhengzhong Kreth, Jens Merritt, Justin Front Microbiol Microbiology Regulated RNA turnover is vital for the control of gene expression in all cellular life. In Escherichia coli, this process is largely controlled by a stable degradosome complex containing RNase E and a variety of additional enzymes. In the Firmicutes phylum, species lack RNase E and often encode the paralogous enzymes RNase J1 and RNase J2. Unlike RNase J1, surprisingly little is known about the regulatory function and protein interactions of RNase J2, despite being a central pleiotropic regulator for the streptococci and other closely related organisms. Using crosslink coimmunoprecipitation in Streptococcus mutans, we have identified the major proteins found within RNase J2 protein complexes located in the cytoplasm and at the cell membrane. In both subcellular fractions, RNase J2 exhibited the most robust interactions with RNase J1, while additional transient and/or weaker “degradosome-like” interactions were also detected. In addition, RNase J2 exhibits multiple novel interactions that have not been previously reported for any RNase J proteins, some of which were highly biased for either the cytoplasmic or membrane fractions. We also determined that the RNase J2 C-terminal domain (CTD) encodes a structure that is likely conserved among RNase J enzymes and may have an analogous function to the C-terminal portion of RNase E. While we did observe a number of parallels between the RNase J2 interactome and the E. coli degradosome paradigm, our results suggest that S. mutans degradosomes are either unlikely to exist or are quite distinct from those of E. coli. Frontiers Media S.A. 2019-09-18 /pmc/articles/PMC6759994/ /pubmed/31620106 http://dx.doi.org/10.3389/fmicb.2019.02150 Text en Copyright © 2019 Mu, Shinde, Zou, Kreth and Merritt. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Microbiology
Mu, Rong
Shinde, Pushkar
Zou, Zhengzhong
Kreth, Jens
Merritt, Justin
Examining the Protein Interactome and Subcellular Localization of RNase J2 Complexes in Streptococcus mutans
title Examining the Protein Interactome and Subcellular Localization of RNase J2 Complexes in Streptococcus mutans
title_full Examining the Protein Interactome and Subcellular Localization of RNase J2 Complexes in Streptococcus mutans
title_fullStr Examining the Protein Interactome and Subcellular Localization of RNase J2 Complexes in Streptococcus mutans
title_full_unstemmed Examining the Protein Interactome and Subcellular Localization of RNase J2 Complexes in Streptococcus mutans
title_short Examining the Protein Interactome and Subcellular Localization of RNase J2 Complexes in Streptococcus mutans
title_sort examining the protein interactome and subcellular localization of rnase j2 complexes in streptococcus mutans
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6759994/
https://www.ncbi.nlm.nih.gov/pubmed/31620106
http://dx.doi.org/10.3389/fmicb.2019.02150
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