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The Staphylococcal Accessory Regulator, SarA, is an RNA-Binding Protein that Modulates the mRNA Turnover Properties of Late-Exponential and Stationary Phase Staphylococcus aureus Cells
The modulation of mRNA turnover is gaining recognition as a mechanism by which Staphylococcus aureus regulates gene expression, but the factors that orchestrate alterations in transcript degradation are poorly understood. In that regard, we previously found that 138 mRNA species, including transcrip...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Research Foundation
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3417590/ https://www.ncbi.nlm.nih.gov/pubmed/22919618 http://dx.doi.org/10.3389/fcimb.2012.00026 |
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author | Morrison, John M. Anderson, Kelsi L. Beenken, Karen E. Smeltzer, Mark S. Dunman, Paul M. |
author_facet | Morrison, John M. Anderson, Kelsi L. Beenken, Karen E. Smeltzer, Mark S. Dunman, Paul M. |
author_sort | Morrison, John M. |
collection | PubMed |
description | The modulation of mRNA turnover is gaining recognition as a mechanism by which Staphylococcus aureus regulates gene expression, but the factors that orchestrate alterations in transcript degradation are poorly understood. In that regard, we previously found that 138 mRNA species, including transcripts coding for the virulence factors protein A (spa) and collagen-binding protein (cna), are stabilized in a sarA-dependent manner during exponential phase growth, suggesting that SarA directly or indirectly affects the RNA turnover properties of these transcripts. Herein, we expanded our characterization of the effects of sarA on mRNA turnover during late-exponential and stationary phases of growth. Results revealed that the locus affects the RNA degradation properties of cells during both growth phases. Further, using gel mobility shift assays and RIP-Chip, it was found that SarA protein is capable of binding mRNA species that it stabilizes both in vitro and within bacterial cells. Taken together, these results suggest that SarA post-transcriptionally regulates S. aureus gene expression in a manner that involves binding to and consequently altering the mRNA turnover properties of target transcripts. |
format | Online Article Text |
id | pubmed-3417590 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Frontiers Research Foundation |
record_format | MEDLINE/PubMed |
spelling | pubmed-34175902012-08-23 The Staphylococcal Accessory Regulator, SarA, is an RNA-Binding Protein that Modulates the mRNA Turnover Properties of Late-Exponential and Stationary Phase Staphylococcus aureus Cells Morrison, John M. Anderson, Kelsi L. Beenken, Karen E. Smeltzer, Mark S. Dunman, Paul M. Front Cell Infect Microbiol Microbiology The modulation of mRNA turnover is gaining recognition as a mechanism by which Staphylococcus aureus regulates gene expression, but the factors that orchestrate alterations in transcript degradation are poorly understood. In that regard, we previously found that 138 mRNA species, including transcripts coding for the virulence factors protein A (spa) and collagen-binding protein (cna), are stabilized in a sarA-dependent manner during exponential phase growth, suggesting that SarA directly or indirectly affects the RNA turnover properties of these transcripts. Herein, we expanded our characterization of the effects of sarA on mRNA turnover during late-exponential and stationary phases of growth. Results revealed that the locus affects the RNA degradation properties of cells during both growth phases. Further, using gel mobility shift assays and RIP-Chip, it was found that SarA protein is capable of binding mRNA species that it stabilizes both in vitro and within bacterial cells. Taken together, these results suggest that SarA post-transcriptionally regulates S. aureus gene expression in a manner that involves binding to and consequently altering the mRNA turnover properties of target transcripts. Frontiers Research Foundation 2012-03-08 /pmc/articles/PMC3417590/ /pubmed/22919618 http://dx.doi.org/10.3389/fcimb.2012.00026 Text en Copyright © 2012 Morrison, Anderson, Beenken, Smeltzer and Dunman. http://www.frontiersin.org/licenseagreement This is an open-access article distributed under the terms of the Creative Commons Attribution Non Commercial License, which permits non-commercial use, distribution, and reproduction in other forums, provided the original authors and source are credited. |
spellingShingle | Microbiology Morrison, John M. Anderson, Kelsi L. Beenken, Karen E. Smeltzer, Mark S. Dunman, Paul M. The Staphylococcal Accessory Regulator, SarA, is an RNA-Binding Protein that Modulates the mRNA Turnover Properties of Late-Exponential and Stationary Phase Staphylococcus aureus Cells |
title | The Staphylococcal Accessory Regulator, SarA, is an RNA-Binding Protein that Modulates the mRNA Turnover Properties of Late-Exponential and Stationary Phase Staphylococcus aureus Cells |
title_full | The Staphylococcal Accessory Regulator, SarA, is an RNA-Binding Protein that Modulates the mRNA Turnover Properties of Late-Exponential and Stationary Phase Staphylococcus aureus Cells |
title_fullStr | The Staphylococcal Accessory Regulator, SarA, is an RNA-Binding Protein that Modulates the mRNA Turnover Properties of Late-Exponential and Stationary Phase Staphylococcus aureus Cells |
title_full_unstemmed | The Staphylococcal Accessory Regulator, SarA, is an RNA-Binding Protein that Modulates the mRNA Turnover Properties of Late-Exponential and Stationary Phase Staphylococcus aureus Cells |
title_short | The Staphylococcal Accessory Regulator, SarA, is an RNA-Binding Protein that Modulates the mRNA Turnover Properties of Late-Exponential and Stationary Phase Staphylococcus aureus Cells |
title_sort | staphylococcal accessory regulator, sara, is an rna-binding protein that modulates the mrna turnover properties of late-exponential and stationary phase staphylococcus aureus cells |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3417590/ https://www.ncbi.nlm.nih.gov/pubmed/22919618 http://dx.doi.org/10.3389/fcimb.2012.00026 |
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