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https://hdl.handle.net/1822/31856
Título: | Halorhabdus tiamatea : proteogenomics and glycosidase activity measurements identify the first cultivated euryarchaeon from a deep-sea anoxic brine lake as potential polysaccharide degrader |
Autor(es): | Werner, Johannes Ferrer, Manuel Michel, Gurvan Mann, Alexander J. Sixing Huang Juarez, Silvia Ciordia, Sergio Albar, Juan P. Alcaide, María La Cono, Violetta Yakimov, Michail M. Antunes, André Guimarães Lemos Taborda, Marco Costa, Milton S. da Tran Hai Glöckner, Frank Oliver Golyshina, Olga V. Golyshin, Peter N. Teeling, Hanno The MAMBA Consortium |
Data: | 2014 |
Editora: | Blackwell Publishing Inc. |
Revista: | Applied and Environmental Microbiology |
Citação: | Werner, Johannes; Ferrer, Manuel; Michel, Gurvan; Mann, Alexander J.; Huang, Sixing; Juarez, Silvia; Ciordia, Sergio; Albar, Juan P.; Alcaide, María; La Cono, Violetta; Yakimov, Michail M.; Antunes, A.; Taborda, Marco; da Costa, Milton S.; Hai, Tran; Glöckner, Frank Oliver; Golyshina, Olga V.; Golyshin, Peter N.; Teeling, Hanno; The MAMBA Consortium, Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements identify the first cultivated euryarchaeon from a deep-sea anoxic brine lake as potential polysaccharide degrader. Environmental Microbiology, 16(8), 2525-2537, 2014 |
Resumo(s): | Euryarchaea from the genus Halorhabdus have been found in hypersaline habitats worldwide, yet are represented by only two isolates: Halorhabdus utahensis AX-2T from the shallow Great Salt Lake of Utah, and Halorhabdus tiamatea SARL4BT from the Shaban deep-sea hypersaline anoxic lake (DHAL) in the Red Sea. We sequenced the H. tiamatea genome to elucidate its niche adaptations. Among sequenced archaea, H. tiamatea features the highest number of glycoside hydrolases, the majority of which were expressed in proteome experiments. Annotations and glycosidase activity measurements suggested an adaptation towards recalcitrant algal and plant-derived hemicelluloses. Glycosidase activities were higher at 2% than at 0% or 5% oxygen, supporting a preference for low-oxygen conditions. Likewise, proteomics indicated quinone-mediated electron transport at 2% oxygen, but a notable stress response at 5% oxygen. Halorhabdus tiamatea furthermore encodes proteins characteristic for thermophiles and light-dependent enzymes (e.g. bacteriorhodopsin), suggesting that H. tiamatea evolution was mostly not governed by a cold, dark, anoxic deep-sea habitat. Using enrichment and metagenomics, we could demonstrate presence of similar glycoside hydrolase-rich Halorhabdus members in the Mediterranean DHAL Medee, which supports that Halorhabdus species can occupy a distinct niche as polysaccharide degraders in hypersaline environments. |
Tipo: | Artigo |
URI: | https://hdl.handle.net/1822/31856 |
DOI: | 10.1111/1462-2920.12393 |
ISSN: | 1462-2912 |
e-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_17984_1.pdf | 657,63 kB | Adobe PDF | Ver/Abrir |