GeLC-MS-based proteomics of Chromobacterium violaceum: comparison of proteome changes elicited by hydrogen peroxide.
Chromobacterium violaceum is a free-living bacillus with several genes that enables it survival under different harsh environments such as oxidative and temperature stresses. Here we performed a label-free quantitative proteomic study to unravel the molecular mechanisms that enable C. violaceum to survive oxidative stress. To achieve this, total proteins extracted from control and C. violaceum cultures exposed during two hours with 8 mM hydrogen peroxide were analyzed using GeLC-MS proteomics. Analysis revealed that under the stress condition, the bacterium expressed proteins that protected it from the damage caused by reactive oxygen condition and decreasing the abundance of proteins responsible for bacterial growth and catabolism. GeLC-MS proteomics analysis provided an overview of the metabolic pathways involved in the response of C. violaceum to oxidative stress ultimately aggregating knowledge of the response of this organism to environmental stress. This study identified approximately 1500 proteins, generating the largest proteomic coverage of C. violaceum so far. We also detected proteins with unknown function that we hypothesize to be part of new mechanisms related to oxidative stress defense. Finally, we identified the mechanism of clustered regularly interspaced short palindromic repeats (CRISPR), which has not yet been reported for this organism.
Laboratório de Biologia Molecular e Genômica, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Campus Universitário s/n, Lagoa Nova, Natal, RN, 59072-970 Brazil.
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Lima
Instituto Federal de Educação, Ciência e Tecnologia do Rio Grande do Norte (IFRN), RN, Brazil.
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Duarte
Colegiado de Medicina, Universidade Federal do Vale do São Francisco, Avenida José de Sá Maniçoba, S/N, Centro, Petrolina, PE, 56304-917, Brazil.
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Medeiros
Laboratório de Proteômica e Engenharia de Proteínas, Instituto Carlos Chagas, Fiocruz, PR, Brazil.
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Carvalho
Unidade Proteômica, Laboratório de Química de Proteínas, Bloco A - sala 543, Centro de Tecnologia, Universidade Federal do Rio de Janeiro, Av. Athos da Silveira Ramos, 149, Cidade Universitária, Rio de Janeiro, RJ, 21941 - 909, Brazil.
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Nogueira
Unidade Proteômica, Laboratório de Química de Proteínas, Bloco A - sala 543, Centro de Tecnologia, Universidade Federal do Rio de Janeiro, Av. Athos da Silveira Ramos, 149, Cidade Universitária, Rio de Janeiro, RJ, 21941 - 909, Brazil.
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Araujo
Unidade Proteômica, Laboratório de Química de Proteínas, Bloco A - sala 543, Centro de Tecnologia, Universidade Federal do Rio de Janeiro, Av. Athos da Silveira Ramos, 149, Cidade Universitária, Rio de Janeiro, RJ, 21941 - 909, Brazil.
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Domont
Laboratório de Biologia Molecular e Genômica, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Campus Universitário s/n, Lagoa Nova, Natal, RN, 59072-970 Brazil.
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Batistuzzo de Medeiros
D001426:Bacterial Proteins / Q000235:genetics; D001938:Brazil; D002374:Catalase / Q000378:metabolism; D002853:Chromatography, Liquid; D002861:Chromobacterium / Q000235:genetics* / Q000378:metabolism; D064112:Clustered Regularly Interspaced Short Palindromic Repeats / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects* / Q000235:genetics; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D013058:Mass Spectrometry; D018384:Oxidative Stress / Q000235:genetics*; D020543:Proteome / Q000235:genetics*; D040901:Proteomics / Q000379:methods
D001426:Bacterial Proteins; D020543:Proteome; D006861:Hydrogen Peroxide; D002374:Catalase