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Characterization of the RNase R association with ribosomes
BACKGROUND: In this study we employed the TAP tag purification method coupled with mass spectrometry analysis to identify proteins that co-purify with Escherichia coli RNase R during exponential growth and after temperature downshift. RESULTS: Our initial results suggested that RNase R can interact...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3942186/ https://www.ncbi.nlm.nih.gov/pubmed/24517631 http://dx.doi.org/10.1186/1471-2180-14-34 |
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author | Malecki, Michal Bárria, Cátia Arraiano, Cecilia M |
author_facet | Malecki, Michal Bárria, Cátia Arraiano, Cecilia M |
author_sort | Malecki, Michal |
collection | PubMed |
description | BACKGROUND: In this study we employed the TAP tag purification method coupled with mass spectrometry analysis to identify proteins that co-purify with Escherichia coli RNase R during exponential growth and after temperature downshift. RESULTS: Our initial results suggested that RNase R can interact with bacterial ribosomes. We subsequently confirmed this result using sucrose gradient ribosome profiling joined with western blot analysis. We found that RNase R co-migrates with the single 30S ribosomal subunits. Independent data involving RNase R in the rRNA quality control process allowed us to hypothesize that the RNase R connection with ribosomes has an important physiological role. CONCLUSIONS: This study leads us to conclude that RNase R can interact with ribosomal proteins and that this interaction may be a result of this enzyme involvement in the ribosome quality control. |
format | Online Article Text |
id | pubmed-3942186 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-39421862014-03-05 Characterization of the RNase R association with ribosomes Malecki, Michal Bárria, Cátia Arraiano, Cecilia M BMC Microbiol Research Article BACKGROUND: In this study we employed the TAP tag purification method coupled with mass spectrometry analysis to identify proteins that co-purify with Escherichia coli RNase R during exponential growth and after temperature downshift. RESULTS: Our initial results suggested that RNase R can interact with bacterial ribosomes. We subsequently confirmed this result using sucrose gradient ribosome profiling joined with western blot analysis. We found that RNase R co-migrates with the single 30S ribosomal subunits. Independent data involving RNase R in the rRNA quality control process allowed us to hypothesize that the RNase R connection with ribosomes has an important physiological role. CONCLUSIONS: This study leads us to conclude that RNase R can interact with ribosomal proteins and that this interaction may be a result of this enzyme involvement in the ribosome quality control. BioMed Central 2014-02-11 /pmc/articles/PMC3942186/ /pubmed/24517631 http://dx.doi.org/10.1186/1471-2180-14-34 Text en Copyright © 2014 Malecki et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. |
spellingShingle | Research Article Malecki, Michal Bárria, Cátia Arraiano, Cecilia M Characterization of the RNase R association with ribosomes |
title | Characterization of the RNase R association with ribosomes |
title_full | Characterization of the RNase R association with ribosomes |
title_fullStr | Characterization of the RNase R association with ribosomes |
title_full_unstemmed | Characterization of the RNase R association with ribosomes |
title_short | Characterization of the RNase R association with ribosomes |
title_sort | characterization of the rnase r association with ribosomes |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3942186/ https://www.ncbi.nlm.nih.gov/pubmed/24517631 http://dx.doi.org/10.1186/1471-2180-14-34 |
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