Utilize este identificador para referenciar este registo: https://hdl.handle.net/1822/42868

TítuloGenome 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.
Data2016
EditoraBlackwell Publishing Inc.
RevistaEnvironmental Microbiology
CitaçãoMehboob, 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.
TipoArtigo
URIhttps://hdl.handle.net/1822/42868
DOI10.1111/1462-2920.12880
ISSN1462-2912
e-ISSN1462-2920
Versão da editorahttp://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1462-2920
Arbitragem científicayes
AcessoAcesso aberto
Aparece nas coleções:CEB - Publicações em Revistas/Séries Internacionais / Publications in International Journals/Series

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