Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements identify the first cultivated euryarchaeon from a deep‐sea anoxic brine lake as potential polysaccharide degrader. (27th February 2014)

• Record Type: Journal Article
• Authors: 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, André; Taborda, Marco; da Costa, Milton S.; Hai, Tran; Glöckner, Frank Oliver; Golyshina, Olga V.; Golyshin, Peter N.; Teeling, Hanno; The MAMBA Consortium
• Is Part Of: Environmental microbiology. Volume 16:Number 8(2014:Aug.)
• Page Start: 2525
• Page End: 2537
• Publication Date: 2014-02-27
• Subjects: Microbial ecology -- Periodicals; Environmental Microbiology -- Periodicals; 579.17
• DOI: 10.1111/1462-2920.12393
• Languages: English
• ISSNs: 1462-2912

Abstract

<abstract abstract-type="main"> <title>Summary</title> <p>Euryarchaea from the genus <italic>H</italic><italic>alorhabdus</italic> have been found in hypersaline habitats worldwide, yet are represented by only two isolates: <italic>H</italic><italic>alorhabdus utahensis</italic> AX‐2<sup>T</sup> from the shallow Great Salt Lake of Utah, and <italic>H</italic><italic>alorhabdus tiamatea</italic> SARL4B<sup>T</sup> from the Shaban deep‐sea hypersaline anoxic lake (DHAL) in the Red Sea. We sequenced the <italic>H</italic><italic>. tiamatea</italic> genome to elucidate its niche adaptations. Among sequenced archaea, <italic>H</italic><italic>. tiamatea</italic> 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. <italic>H</italic><italic>alorhabdus tiamatea</italic> furthermore encodes proteins characteristic for thermophiles and light‐dependent enzymes (e.g. bacteriorhodopsin), suggesting that <italic>H</italic><italic>. tiamatea</italic> 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 <italic>H</italic><italic>alorhabdus</italic> members in the Mediterranean DHAL Medee, which supports that <italic>H</italic><italic>alorhabdus</italic> species can occupy a distinct niche as polysaccharide degraders in hypersaline environments.</p> </abstract>