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https://hdl.handle.net/1822/42868
Título: | Genome and proteome analysis of Pseudomonas chloritidismutans AW-1T that grows on n-decane with chlorate or oxygen as electron acceptor |
Autor(es): | Mehboob, Farrakh Oosterkamp, Margreet J. Koehorst, Jasper J. Farrakh, Sumaira Veuskens, Teun Plugge, Caroline M. Boeren, Sjef Vos, Willem M. de Schraa, Gosse Stams, Alfons Johannes Maria Schaap, Peter J. |
Data: | 2016 |
Editora: | Blackwell Publishing Inc. |
Revista: | Environmental Microbiology |
Citação: | Mehboob, Farrakh; Oosterkamp, Margreet J.; Koehorst, Jasper J.; Farrakh, Sumaira; Veuskens, Teun; Plugge, Caroline M.; Boeren, Sjef; de Vos, Willem M.; Schraa, Gosse; Stams, A. J. M.; Schaap, Peter J., Genome and proteome analysis of Pseudomonas chloritidismutans AW-1T that grows on n-decane with chlorate or oxygen as electron acceptor. Environmental Microbiology, 18(10), 3247-3257, 2016 |
Resumo(s): | Growth of Pseudomonas chloritidismutans AW-1T on C7 to C12 n-alkanes with oxygen or chlorate as electron acceptor was studied by genome and proteome analysis. Whole genome shotgun sequencing resulted in a 5 Mbp assembled sequence with a G+C content of 62.5% The automatic annotation identified 4767 protein-encoding genes and a putative function could be assigned to almost 80% of the predicted proteins. The distinct phylogenetic position of P. chloritidismutans AW-1T within the Pseudomonas stutzeri cluster became clear by comparison of average nucleotide identity values of sequenced genomes. Analysis of the proteome of P. chloritidismutans AW-1T showed the versatility of this bacterium to adapt to aerobic and anaerobic growth conditions with acetate or n-decane as substrates. All enzymes involved in the alkane oxidation pathway were identified. An alkane monooxygenase was detected in n-decane-grown cells, but not in acetate-grown cells. The enzyme was found when grown in the presence of oxygen or chlorate, indicating that under both conditions an oxygenase-mediated pathway is employed for alkane degradation. Proteomic and biochemical data also showed that both chlorate reductase and chlorite dismutase are constitutively present, but most abundant under chlorate-reducing conditions. |
Tipo: | Artigo |
URI: | https://hdl.handle.net/1822/42868 |
DOI: | 10.1111/1462-2920.12880 |
ISSN: | 1462-2912 |
e-ISSN: | 1462-2920 |
Versão da editora: | http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1462-2920 |
Arbitragem científica: | yes |
Acesso: | Acesso aberto |
Aparece nas coleções: | CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series |
Ficheiros deste registo:
Ficheiro | Descrição | Tamanho | Formato | |
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document_19981_1.pdf | 129,42 kB | Adobe PDF | Ver/Abrir |