Persephonella marina gen. nov., sp. nov. and Persephonella guaymasensis sp. nov., two novel, thermophilic, hydrogen-oxidizing microaerophiles from deep-sea hydrothermal vents.

Götz, Dorothee; Banta, Amy B.; Beveridge, Terry J.; Rushdi, A I; Simoneit, Bernd R.T.; Reysenbach, A.-L.

doi:10.1099/00207713-52-4-1349

Cited by 80 publications

(55 citation statements)

References 41 publications

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“…Catalytic performance of P. marina P RNA was lower, with approximately a sevenfold increase in K m(sto) and a 31-fold decrease in k react . Since the two Aquificales are thermophilic bacteria (growth optima z70°C; Götz et al 2002;Aguiar et al 2004), we tested processing activity at two additional temperatures (55°C and 65°C), using P RNA concentrations (0.27 mM for E. coli, 0.27 mM for S. azorense, and 2.0 mM for P. marina) around the respective K m(sto) value determined at 37°C (see Table 1). For this purpose, P RNAs were preincubated in assay buffer for 1 h at 55°C or 65°C before addition of substrate and incubation at the same temperature.…”

Section: P Rna Structures and Kineticsmentioning

confidence: 99%

Thermostable RNase P RNAs lacking P18 identified in the Aquificales

Marszalkowski¹,

Teune²,

Steger³

et al. 2006

RNA

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The RNase P RNA (rnpB) and protein (rnpA) genes were identified in the two Aquificales Sulfurihydrogenibium azorense and Persephonella marina. In contrast, neither of the two genes has been found in the sequenced genome of their close relative, Aquifex aeolicus. As in most bacteria, the rnpA genes of S. azorense and P. marina are preceded by the rpmH gene coding for ribosomal protein L34. This genetic region, including several genes up-and downstream of rpmH, is uniquely conserved among all three Aquificales strains, except that rnpA is missing in A. aeolicus. The RNase P RNAs (P RNAs) of S. azorense and P. marina are active catalysts that can be activated by heterologous bacterial P proteins at low salt. Although the two P RNAs lack helix P18 and thus one of the three major interdomain tertiary contacts, they are more thermostable than Escherichia coli P RNA and require higher temperatures for proper folding. Related to their thermostability, both RNAs include a subset of structural idiosyncrasies in their S domains, which were recently demonstrated to determine the folding properties of the thermostable S domain of Thermus thermophilus P RNA. Unlike 16S rRNA phylogeny that has placed the Aquificales as the deepest lineage of the bacterial phylogenetic tree, RNase P RNA-based phylogeny groups S. azorense and P. marina with the green sulfur, cyanobacterial, and d/e proteobacterial branches.

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Section: P Rna Structures and Kineticsmentioning

confidence: 99%

Thermostable RNase P RNAs lacking P18 identified in the Aquificales

Marszalkowski¹,

Teune²,

Steger³

et al. 2006

RNA

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“…On the other hand, the accumulation of GG had been detected only in mesophilic bacteria and archaea (8,21,26,33). However, GG was recently shown to accumulate in Persephonella marina (H. Santos, personal communication), a thermophilic, strictly chemolithoautotrophic, microaerophilic, hydrogen-oxidizing bacterium isolated from a deep-sea hydrothermal vent which is a member of the order Aquificales (20). This bacterium has a temperature range for growth of between 55 and 80°C (optimum at 73°C) and grows optimally in media containing 2.5% (wt/vol) NaCl (20).…”

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confidence: 99%

“…However, GG was recently shown to accumulate in Persephonella marina (H. Santos, personal communication), a thermophilic, strictly chemolithoautotrophic, microaerophilic, hydrogen-oxidizing bacterium isolated from a deep-sea hydrothermal vent which is a member of the order Aquificales (20). This bacterium has a temperature range for growth of between 55 and 80°C (optimum at 73°C) and grows optimally in media containing 2.5% (wt/vol) NaCl (20). The identification of GG in this organism, where it may have a role in osmoadaptation, prompted us to examine the pathway for its synthesis.…”

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confidence: 99%

Glucosylglycerate Biosynthesis in the Deepest Lineage of the Bacteria : Characterization of the Thermophilic Proteins GpgS and GpgP from Persephonella marina

2007

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The pathway for the synthesis of glucosylglycerate (GG) in the thermophilic bacterium Persephonella marina is proposed based on the activities of recombinant glucosyl-3-phosphoglycerate (GPG) synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP). The sequences of gpgS and gpgP from the cold-adapted bacterium Methanococcoides burtonii were used to identify the homologues in the genome of P. marina, which were separately cloned and overexpressed as His-tagged proteins in Escherichia coli. The recombinant GpgS protein of P. marina, unlike the homologue from M. burtonii, which was specific for GDP-glucose, catalyzed the synthesis of GPG from UDP-glucose, GDP-glucose, ADP-glucose, and TDP-glucose (in order of decreasing efficiency) and from D-3-phosphoglycerate, with maximal activity at 90°C. The recombinant GpgP protein, like the M. burtonii homologue, dephosphorylated GPG and mannosyl-3-phosphoglycerate (MPG) to GG and mannosylglycerate, respectively, yet at high temperatures the hydrolysis of GPG was more efficient than that of MPG. Gel filtration indicates that GpgS is a dimeric protein, while GpgP is monomeric. This is the first characterization of genes and enzymes for the synthesis of GG in a thermophile.The compatible solute ␣-glucosylglycerate (GG) has been identified in the cyanobacterium Agmenellum quadruplicatum strain PCC7002, in the archaeon Methanohalophilus portucalensis strain FDF-1, in a salt-sensitive mutant of Halomonas elongata, and in the ␥-proteobacterium Erwinia chrysanthemi strain 3937, where it behaves as a compatible solute during osmotic stress under nitrogen-limiting conditions (8,21,26,33). This compatible solute is chemically related to mannosylglycerate (MG), which is widespread in (hyper)thermophilic bacteria and archaea and has been shown to serve as a compatible solute under salt stress in several of these organisms (1,35,36). However, MG has also been encountered in marine red algae, and the genes for the synthesis of MG have been found in the mesophilic bacterium "Dehalococcoides ethenogenes" (proposed name) (16,25). On the other hand, the accumulation of GG had been detected only in mesophilic bacteria and archaea (8,21,26,33). However, GG was recently shown to accumulate in Persephonella marina (H. Santos, personal communication), a thermophilic, strictly chemolithoautotrophic, microaerophilic, hydrogen-oxidizing bacterium isolated from a deep-sea hydrothermal vent which is a member of the order Aquificales (20). This bacterium has a temperature range for growth of between 55 and 80°C (optimum at 73°C) and grows optimally in media containing 2.5% (wt/vol) NaCl (20). The identification of GG in this organism, where it may have a role in osmoadaptation, prompted us to examine the pathway for its synthesis.The biosynthetic pathway for the synthesis of GG in Methanococcoides burtonii proceeds via a two-step pathway involving glucosyl-3-phosphoglycerate synthase (GpgS), which catalyzes the conversion of GDP-glucose and D-3-phosphoglycerate (3-PGA) to glucosyl-3-phosphogl...

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“…Based on molecular ecological analyses, the Aquificales species appear to be dominant members of communities in near-neutral hot springs in Japan, 22) Iceland, 23) and Yellowstone National Park, 24,25) and in shallow marine hydrothermal systems, 26) where sulfur compounds are available. All seven species are known to be capable of utilizing thiosulfate as an electron donor, [27][28][29] and hence it is plausible that such species conserve sulfur oxidation enzymes.…”

Section: Resultsmentioning

confidence: 99%