Details zur Publikation

Referenztyp Zeitschriften
DOI / URL Link
Titel (primär) Metaproteogenomic analysis of a sulfate-reducing enrichment culture reveals genomic organization of key enzymes in the m-xylene degradation pathway and metabolic activity of proteobacteria
Autor Bozinovski, D.; Taubert, M.; Kleinsteuber, S.; Richnow, H.-H.; von Bergen, M.; Vogt, C.; Seifert, J.;
Journal / Serie Systematic and Applied Microbiology
Erscheinungsjahr 2014
Department ISOBIO; UMB; PROTEOM;
Band/Volume 37
Heft 7
Sprache englisch;
POF III (gesamt) T41;
Keywords Anaerobic m-xylene degradation; Metaproteomics; Mass spectrometry; Protein-SIP
UFZ Querschnittsthemen RU3;
Abstract This study aimed to ascertain the functional and phylogenetic relationships within an m-xylene degrading sulfate-reducing enrichment culture, which had been maintained for several years in the laboratory with m-xylene as the sole source of carbon and energy. Previous studies indicated that a phylotype affiliated to the Desulfobacteraceae was the main m-xylene assimilating organism. In the present study, genes and gene products were identified by a metaproteogenomic approach using LC-MS/MS analysis of the microbial community, and 2426 peptides were identified from 576 proteins. In the metagenome of the community, gene clusters encoding enzymes involved in fumarate addition to a methyl moiety of m-xylene (nms, bss), as well as gene clusters coding for enzymes involved in modified beta-oxidation to (3-methyl)benzoyl-CoA (bns), were identified in two separate contigs. Additionally, gene clusters containing homologues to bam genes encoding benzoyl-CoA reductase (Bcr) class II, catalyzing the dearomatization of (3-methyl)benzoyl-CoA, were identified. Time-resolved protein stable isotope probing (protein-SIP) experiments using 13C-labeled m-xylene showed that the respective gene products were highly 13C-labeled. The present data suggested the identification of gene products that were similar to those involved in methylnaphthalene degradation even though the consortium was not capable of growing in the presence of naphthalene, methylnaphthalene or toluene as substrates. Thus, a novel branch of enzymes was found that was probably specific for anaerobic m-xylene degradation.
ID 15214
dauerhafte UFZ-Verlinkung https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=15214
Bozinovski, D., Taubert, M., Kleinsteuber, S., Richnow, H.-H., von Bergen, M., Vogt, C., Seifert, J. (2014):
Metaproteogenomic analysis of a sulfate-reducing enrichment culture reveals genomic organization of key enzymes in the m-xylene degradation pathway and metabolic activity of proteobacteria
Syst. Appl. Microbiol. 37 (7), 488 - 501