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Genome and proteome analysis of Pseudomonas chloritidismutans AW‐1T that grows on n‐decane with chlorate or oxygen as electron acceptor

Mehboob, Farrakh, Oosterkamp, Margreet J., Koehorst, Jasper J., Farrakh, Sumaira, Veuskens, Teun, Plugge, Caroline M., Boeren, Sjef, de Vos, Willem M., Schraa, Gosse, Stams, Alfons J.M., Schaap, Peter J.
Environmental microbiology 2016 v.18 no.10 pp. 3247-3257
Pseudomonas stutzeri, acetates, alkanes, bacteria, enzymes, genes, oxidation, oxygen, phylogeny, proteins, proteome, proteomics, sequence analysis
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.