@ARTICLE{TreeBASE2Ref24972,
author = {Fernando Hayashi Sant'Anna and Alexander V Lebedinsky and Tatyana G Sokolova and Frank T Robb and Juan M Gonzalez},
title = {Analysis of three genomes within the thermophilic bacterial species Caldanaerobacter subterraneus with a focus on carbon monoxide dehydrogenase evolution and hydrolase diversity},
year = {2015},
keywords = {Caldanaerobacter subterraneus; genome; horizontal gene transfer; hydrogenase; carbon monoxide dehydrogenase; glycosidase; protease, esterase; phylogeny; thermophile},
doi = {},
url = {http://},
pmid = {},
journal = {BMC Genomics},
volume = {},
number = {},
pages = {},
abstract = {Background
The Caldanaerobacter subterraneus species includes thermophilic fermentative bacteria able to grow on
carbohydrates substrates with acetate and L-alanine as the main products. In this study, comprehensive analysis of
three genomes of C. subterraneus subspecies was carried in order to identify genes encoding key metabolic
enzymes and to document the genomic basis for the evolution of these organisms.
Results
The three genomes of C. subterraneus showed high similarity, although there are substantial differences in their gene
composition and organization. Each subspecies possesses a gene cluster encoding a carbon monoxide
dehydrogenase (CODH) and an energy converting hydrogenase (ECH). The CODH gene is associated with an
operon that resembles the Escherichia coli hydrogenase hyc/hyf operons, a novel genetic context distinct from that
found in archetypical hydrogenogenic carboxydotrophs. Apart from the CODH-associated hydrogenase, these
bacteria also contain other hydrogenases, encoded by ech and hyd genes. An Mbx ferredoxin:NADP oxidoreductase
homolog similar to that originally described in the archaeon Pyrococcus furiosus was uniquely encoded in the C.
subterraneus subsp. yonseiensis genome. Compositional analysis demonstrated that some genes of the CODH-ECH
and mbx operons present distinct sequence patterns in relation to the majority of the other genes of each genome.
Phylogenetic reconstructions of the genes from these operons and those from the ech operon are incongruent to the
species tree. Notably, the cooS gene of C. subterraneus subsp. pacificus and its homologs in C. subterraneus subsp.
tengcongensis and C. subterraneus subsp. yonseiensis form distinct clades. The strains have diverse hydrolytic
enzymes and they appear to be proteolytic and glycolytic. Divergent glycosidases from fourteen families, among them
amylases, chitinases, alpha-glucosidases, beta-glucosidases, and cellulases, were identified. Each of the three
genomes also contains around one hundred proteases from fifty subfamilies, as well about ten different esterases.
Conclusions
Genomic information suggests that multiple horizontal gene transfers conferred the adaptation of C. subterraneus
subspecies to extreme niches throughout the carbon monoxide utilization and hydrogen production. The variety of
hydrolases found in their genomes indicate the versatility of the species in obtaining energy and carbon from diverse
substrates, therefore these organisms constitute a remarkable resource of enzymes with biotechnological potential.}
}
Citation title: "Analysis of three genomes within the thermophilic bacterial species Caldanaerobacter subterraneus with a focus on carbon monoxide dehydrogenase evolution and hydrolase diversity".
Study name: "Analysis of three genomes within the thermophilic bacterial species Caldanaerobacter subterraneus with a focus on carbon monoxide dehydrogenase evolution and hydrolase diversity".
This study is part of submission 18113
(Status: Published).
Citation title: "Analysis of three genomes within the thermophilic bacterial species Caldanaerobacter subterraneus with a focus on carbon monoxide dehydrogenase evolution and hydrolase diversity".
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