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Proteomic analysis of Chromobacterium violaceum and its adaptability to stress
BACKGROUND: Chromobacterium violaceum (C. violaceum) occurs abundantly in a variety of ecosystems, including ecosystems that place the bacterium under stress. This study assessed the adaptability of C. violaceum by submitting it to nutritional and pH stresses and then analyzing protein expression us...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4666173/ https://www.ncbi.nlm.nih.gov/pubmed/26627076 http://dx.doi.org/10.1186/s12866-015-0606-2 |
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author | Castro, Diogo Cordeiro, Isabelle Bezerra Taquita, Paula Eberlin, Marcos Nogueira Garcia, Jerusa Simone Souza, Gustavo Henrique M. F. Arruda, Marco Aurélio Zezzi Andrade, Edmar V. Filho, Spartaco A. Crainey, J. Lee Lozano, Luis Lopez Nogueira, Paulo A. Orlandi, Patrícia P. |
author_facet | Castro, Diogo Cordeiro, Isabelle Bezerra Taquita, Paula Eberlin, Marcos Nogueira Garcia, Jerusa Simone Souza, Gustavo Henrique M. F. Arruda, Marco Aurélio Zezzi Andrade, Edmar V. Filho, Spartaco A. Crainey, J. Lee Lozano, Luis Lopez Nogueira, Paulo A. Orlandi, Patrícia P. |
author_sort | Castro, Diogo |
collection | PubMed |
description | BACKGROUND: Chromobacterium violaceum (C. violaceum) occurs abundantly in a variety of ecosystems, including ecosystems that place the bacterium under stress. This study assessed the adaptability of C. violaceum by submitting it to nutritional and pH stresses and then analyzing protein expression using bi-dimensional electrophoresis (2-DE) and Maldi mass spectrometry. RESULTS: Chromobacterium violaceum grew best in pH neutral, nutrient-rich medium (reference conditions); however, the total protein mass recovered from stressed bacteria cultures was always higher than the total protein mass recovered from our reference culture. The diversity of proteins expressed (repressed by the number of identifiable 2-DE spots) was seen to be highest in the reference cultures, suggesting that stress reduces the overall range of proteins expressed by C. violaceum. Database comparisons allowed 43 of the 55 spots subjected to Maldi mass spectrometry to be characterized as containing a single identifiable protein. Stress-related expression changes were noted for C. violaceum proteins related to the previously characterized bacterial proteins: DnaK, GroEL-2, Rhs, EF-Tu, EF-P; MCP, homogentisate 1,2-dioxygenase, Arginine deiminase and the ATP synthase β-subunit protein as well as for the ribosomal protein subunits L1, L3, L5 and L6. The ability of C. violaceum to adapt its cellular mechanics to sub-optimal growth and protein production conditions was well illustrated by its regulation of ribosomal protein subunits. With the exception of the ribosomal subunit L3, which plays a role in protein folding and maybe therefore be more useful in stressful conditions, all the other ribosomal subunit proteins were seen to have reduced expression in stressed cultures. Curiously, C. violeaceum cultures were also observed to lose their violet color under stress, which suggests that the violacein pigment biosynthetic pathway is affected by stress. CONCLUSIONS: Analysis of the proteomic signatures of stressed C. violaceum indicates that nutrient-starvation and pH stress can cause changes in the expression of the C. violaceum receptors, transporters, and proteins involved with biosynthetic pathways, molecule recycling, energy production. Our findings complement the recent publication of the C. violeaceum genome sequence and could help with the future commercial exploitation of C. violeaceum. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12866-015-0606-2) contains supplementary material, which is available to authorized users. |
format | Online Article Text |
id | pubmed-4666173 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-46661732015-12-02 Proteomic analysis of Chromobacterium violaceum and its adaptability to stress Castro, Diogo Cordeiro, Isabelle Bezerra Taquita, Paula Eberlin, Marcos Nogueira Garcia, Jerusa Simone Souza, Gustavo Henrique M. F. Arruda, Marco Aurélio Zezzi Andrade, Edmar V. Filho, Spartaco A. Crainey, J. Lee Lozano, Luis Lopez Nogueira, Paulo A. Orlandi, Patrícia P. BMC Microbiol Research Article BACKGROUND: Chromobacterium violaceum (C. violaceum) occurs abundantly in a variety of ecosystems, including ecosystems that place the bacterium under stress. This study assessed the adaptability of C. violaceum by submitting it to nutritional and pH stresses and then analyzing protein expression using bi-dimensional electrophoresis (2-DE) and Maldi mass spectrometry. RESULTS: Chromobacterium violaceum grew best in pH neutral, nutrient-rich medium (reference conditions); however, the total protein mass recovered from stressed bacteria cultures was always higher than the total protein mass recovered from our reference culture. The diversity of proteins expressed (repressed by the number of identifiable 2-DE spots) was seen to be highest in the reference cultures, suggesting that stress reduces the overall range of proteins expressed by C. violaceum. Database comparisons allowed 43 of the 55 spots subjected to Maldi mass spectrometry to be characterized as containing a single identifiable protein. Stress-related expression changes were noted for C. violaceum proteins related to the previously characterized bacterial proteins: DnaK, GroEL-2, Rhs, EF-Tu, EF-P; MCP, homogentisate 1,2-dioxygenase, Arginine deiminase and the ATP synthase β-subunit protein as well as for the ribosomal protein subunits L1, L3, L5 and L6. The ability of C. violaceum to adapt its cellular mechanics to sub-optimal growth and protein production conditions was well illustrated by its regulation of ribosomal protein subunits. With the exception of the ribosomal subunit L3, which plays a role in protein folding and maybe therefore be more useful in stressful conditions, all the other ribosomal subunit proteins were seen to have reduced expression in stressed cultures. Curiously, C. violeaceum cultures were also observed to lose their violet color under stress, which suggests that the violacein pigment biosynthetic pathway is affected by stress. CONCLUSIONS: Analysis of the proteomic signatures of stressed C. violaceum indicates that nutrient-starvation and pH stress can cause changes in the expression of the C. violaceum receptors, transporters, and proteins involved with biosynthetic pathways, molecule recycling, energy production. Our findings complement the recent publication of the C. violeaceum genome sequence and could help with the future commercial exploitation of C. violeaceum. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12866-015-0606-2) contains supplementary material, which is available to authorized users. BioMed Central 2015-12-01 /pmc/articles/PMC4666173/ /pubmed/26627076 http://dx.doi.org/10.1186/s12866-015-0606-2 Text en © Castro et al. 2015 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated. |
spellingShingle | Research Article Castro, Diogo Cordeiro, Isabelle Bezerra Taquita, Paula Eberlin, Marcos Nogueira Garcia, Jerusa Simone Souza, Gustavo Henrique M. F. Arruda, Marco Aurélio Zezzi Andrade, Edmar V. Filho, Spartaco A. Crainey, J. Lee Lozano, Luis Lopez Nogueira, Paulo A. Orlandi, Patrícia P. Proteomic analysis of Chromobacterium violaceum and its adaptability to stress |
title | Proteomic analysis of Chromobacterium violaceum and its adaptability to stress |
title_full | Proteomic analysis of Chromobacterium violaceum and its adaptability to stress |
title_fullStr | Proteomic analysis of Chromobacterium violaceum and its adaptability to stress |
title_full_unstemmed | Proteomic analysis of Chromobacterium violaceum and its adaptability to stress |
title_short | Proteomic analysis of Chromobacterium violaceum and its adaptability to stress |
title_sort | proteomic analysis of chromobacterium violaceum and its adaptability to stress |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4666173/ https://www.ncbi.nlm.nih.gov/pubmed/26627076 http://dx.doi.org/10.1186/s12866-015-0606-2 |
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