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H alorhabdus tiamatea: proteogenomics and glycosidase activity measurements identify the first cultivated euryarchaeon from a deep‐sea anoxic brine lake as potential polysaccharide degrader
Author(s) -
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,
Costa Milton S.,
Hai Tran,
Glöckner Frank Oliver,
Golyshina Olga V.,
Golyshin Peter N.,
Teeling Hanno
Publication year - 2014
Publication title -
environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.954
H-Index - 188
eISSN - 1462-2920
pISSN - 1462-2912
DOI - 10.1111/1462-2920.12393
Subject(s) - biology , anoxic waters , glycoside hydrolase , thermophile , proteome , metaproteomics , extreme environment , archaea , halophile , metagenomics , botany , ecology , biochemistry , bacteria , enzyme , gene , genetics
Summary Euryarchaea from the genus H alorhabdus have been found in hypersaline habitats worldwide, yet are represented by only two isolates: H alorhabdus utahensis AX ‐2 T from the shallow G reat S alt L ake of U tah, and H alorhabdus tiamatea SARL 4 B T from the S haban deep‐sea hypersaline anoxic lake ( DHAL ) in the R ed S ea. 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. H alorhabdus 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 H alorhabdus members in the M editerranean DHAL M edee, which supports that H alorhabdus species can occupy a distinct niche as polysaccharide degraders in hypersaline environments.