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The gill chamber epibiosis of deep-sea shrimp Rimicaris exoculata: an in-depth metagenomic investigation and discovery of Zetaproteobacteria ArchiMer
Jan, Cyrielle; Petersen, Jillian M.; Werner, Johannes; Teeling, Hanno; Huang, Sixing; Gloeckner, Frank Oliver; Golyshina, Olga V.; Dubilier, Nicole; Golyshin, Peter N.; Jebbar, Mohamed; Cambon-bonavita, Marie-anne.
The gill chamber of deep-sea hydrothermal vent shrimp Rimicaris exoculata hosts a dense community of epibiotic bacteria dominated by filamentous Epsilonproteobacteria and Gammaproteobacteria. Using metagenomics on shrimp from the Rainbow hydrothermal vent field, we showed that both epibiont groups have the potential to grow autotrophically and oxidize reduced sulfur compounds or hydrogen with oxygen or nitrate. For carbon fixation, the Epsilonproteobacteria use the reductive tricarboxylic acid cycle, whereas the Gammaproteobacteria use the Calvin–Benson–Bassham cycle. Only the epsilonproteobacterial epibionts had the genes necessary for producing ammonium. This ability likely minimizes direct competition between epibionts and also broadens the spectrum of...
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Ano: 2014 URL: http://archimer.ifremer.fr/doc/00177/28874/28622.pdf
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Identification and Characterization of Carboxyl Esterases of Gill Chamber-Associated Microbiota in the Deep-Sea Shrimp Rimicaris exoculata by Using Functional Metagenomics ArchiMer
Alcaide, Maria; Tchigvintsev, Anatoli; Martinez-martinez, Monica; Popovic, Ana; Reva, Oleg N.; Lafraya, Alvaro; Bargiela, Rafael; Nechitaylo, Taras Y.; Matesanz, Ruth; Cambon-bonavita, Marie-anne; Jebbar, Mohamed; Yakimov, Michail M.; Savchenko, Alexei; Golyshina, Olga V.; Yakunin, Alexander F.; Golyshin, Peter N.; Ferrer, Manuel.
The shrimp Rimicaris exoculata dominates the fauna in deep-sea hydrothermal vent sites along the Mid-Atlantic Ridge (depth, 2,320 m). Here, we identified and biochemically characterized three carboxyl esterases from microbial communities inhabiting the R. exoculata gill that were isolated by naive screens of a gill chamber metagenomic library. These proteins exhibit low to moderate identity to known esterase sequences (<= 52%) and to each other (11.9 to 63.7%) and appear to have originated from unknown species or from genera of Proteobacteria related to Thiothrix/Leucothrix (MGS-RG1/RG2) and to the Rhodobacteraceae group (MGS-RG3). A library of 131 esters and 31 additional esterase/lipase preparations was used to evaluate the activity profiles of these...
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Ano: 2015 URL: http://archimer.ifremer.fr/doc/00256/36721/36438.pdf
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