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Título: | Proteomics of Syntrophomonas zehnderi and Methanobacterium formicicum growing on long-chain fatty acids |
Autor(es): | Salvador, A. F. Strepis, N. Bize, A. Stams, Alfons Johannes Maria Schaap, Peter J. Alves, M. M. Bouchez, T. Sousa, D. Z. |
Data: | 7-Jun-2015 |
Citação: | Salvador, A. F.; Strepis, N.; Bize, A.; Stams, A. J. M.; Schaap, P.; Alves, M. M.; Bouchez, T.; Sousa, D. Z., Proteomics of Syntrophomonas zehnderi and Methanobacterium formicicum growing on long-chain fatty acids. FEMS 2015 - 6th Congress of European Microbiologists. No. 1988, Maastricht, The Netherlands, June 7-11, 2015. |
Resumo(s): | Background: Conversion of long-chain fatty acids (LCFA) in anaerobic digesters relies on syntrophic relationship between acetogenic bacteria and methanogenic archaea. Conversion of unsaturated- and saturated-LCFA has been previously shown by a coculture of Syntrophomonas zehnderi and Methanobacterium formicium. Degradation of unsaturated-LCFA is rare among Syntrophomonas species; the best studied fatty acid oxidizer, S. wolfei, can only grow on saturated-LCFA. Objectives: Major differences are expected in the pathways and enzymes involved in the degradation of unsaturated-LCFA. In this work we used proteogenomic approach to study these differences. Methods: A draft genome of S. zehnderi was obtained by Illumina HiSeq sequencing. Genomes of S. zehnderi and S. wolfei (available at NCBI) were compared. S. zehnderi and M. formicicum co-cultures grown on oleate (unsaturated LCFA, C18:1) and on stearate (saturated LCFA, C18:0) were further studied using a proteomics approach. Conclusions: Genomic comparison of S. zehnderi and S. wolfei revealed approximately 900 different proteins and 1200 common proteins. In the genome of S. zehnderi, two replicates of the unsaturated acyl-CoA dehydrogenase genes were identified, one of which differs considerably from the acyl-CoA gene found in S. wolfei. Proteomic analysis of S. zehnderi and M. formicium co-cultures revealed high expression levels of proteins related to the -oxidation of LCFA (up to 30% of total proteins identified). Different protein expression levels were observed during the degradation of oleate (44% unique proteins) and stearate (23% unique proteins). In addition, proteins involved in electron transfer were highly expressed, including electron transfer flavoproteins, ATP synthases and a number of hydrogenases and formate dehydrogenases. |
Tipo: | Resumo em ata de conferência |
URI: | https://hdl.handle.net/1822/35810 |
Arbitragem científica: | yes |
Acesso: | Acesso aberto |
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Ficheiro | Descrição | Tamanho | Formato | |
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document_22163_1.pdf | 49,67 kB | Adobe PDF | Ver/Abrir |