LOW MOLECULAR WEIGHT CARBOHYDRATES OF THE BANGIOPHYCIDAE (RHODOPHYTA)<sup>1</sup>

Karsten, Ulf; West, John A.; Zuccarello, Giuseppe C.; Engbrodt, Ralph; Yokoyama, Akiko; Hara, Yoshiaki; Brodie, Juliet

doi:10.1046/j.1529-8817.2003.02192.x

Cited by 61 publications

(59 citation statements)

References 15 publications

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“…The significance of the branching order was evaluated by bootstrap analysis of 1,000 computer-generated trees. (21,22,24,25). We have shown, however, that in the alga Caloglossa leprieurii, the synthesis of MG proceeds in a single-step catalyzed by mannosylglycerate synthase (C. Neves and H. Santos, unpublished data), an alternative biosynthetic pathway, otherwise found only in Rhodothermus marinus; therefore, the synthesis of MG in red algae probably constitutes a particular line that evolved in a restricted number of organisms.…”

Section: Discussionmentioning

confidence: 96%

Compatible Solutes of the HyperthermophilePalaeococcus ferrophilus: Osmoadaptation and Thermoadaptation in the OrderThermococcales

Neves

Costa

Santos

2005

Appl Environ Microbiol

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The effect of salinity and growth temperature on the accumulation of intracellular organic solutes was examined in the hyperthermophilic archaeon Palaeococcus ferrophilus. The genus Palaeococcus represents a deep-branching lineage of the order Thermococcales, which diverged before Thermococcus and Pyrococcus. Palaeococcus ferrophilus accumulated mannosylglycerate, glutamate, and aspartate as major compatible solutes. Unlike members of the genera Pyrococcus and Thermococcus, Palaeococcus ferrophilus did not accumulate di-myo-inositol phosphate, a canonical solute of hyperthermophiles. The level of mannosylglycerate increased in response to both heat and salt stress; glutamate increased at supraoptimal growth temperatures, whereas aspartate increased at supraoptimal salt concentration. Proline, alanine, and trehalose were also found in lesser amounts, but their levels did not respond significantly to any of the stresses imposed. Additionally, the genes involved in the synthesis of mannosylglycerate in Palaeococcus ferrophilus and Thermococcus litoralis were identified. In both organisms the synthesis proceeds via the two-step pathway comprising mannosyl-3-phosphoglycerate synthase (MPGS) (EC 2.4.1.217) and mannosyl-3-phosphoglycerate phosphatase (MPGP) (EC 3.1.3.70). The mpgS and mpgP genes of Palaeococcus ferrophilus were expressed in Escherichia coli and the proteins were characterized. MPGS had maximal activity at 90°C and pH near 7.0, and was strictly dependent on Mg 2؉ . MPGP had optimal activity at 90°C and pH 6.0 and was barely dependent on Mg 2؉ . The half-life values for inactivation of MPGS and MPGP at 83°C were 18 and 25 min, respectively. A comparative discussion of the osmo-and thermoadaptation strategies in these three genera of the Thermococcales is presented.

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Section: Discussionmentioning

confidence: 96%

Compatible Solutes of the HyperthermophilePalaeococcus ferrophilus: Osmoadaptation and Thermoadaptation in the OrderThermococcales

Neves

Costa

Santos

2005

Appl Environ Microbiol

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“…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).…”

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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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“…Mannosylglycerate (MG), di-myo-inositol-phosphate, and diglycerol-phosphate have a more restricted distribution, being found primarily in (hyper)thermophilic prokaryotes. Mannosylglycerate is widespread in (hyper)thermophilic bacteria and archaea and is also found in some red algae (21,35). Cyclic 2,3-bisphosphoglycerate has only been encountered in methanogens (20,25,36).…”

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Characterization of the Biosynthetic Pathway of Glucosylglycerate in the Archaeon Methanococcoides burtonii

et al. 2006

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The pathway for the synthesis of the organic solute glucosylglycerate (GG) is proposed based on the activities of the recombinant glucosyl-3-phosphoglycerate synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP) from Methanococcoides burtonii. A mannosyl-3-phosphoglycerate phosphatase gene homologue (mpgP) was found in the genome of M. burtonii (http://www.jgi.doe.gov), but an mpgS gene coding for mannosyl-3-phosphoglycerate synthase (MpgS) was absent. The gene upstream of the mpgP homologue encoded a putative glucosyltransferase that was expressed in Escherichia coli. The recombinant product had GpgS activity, catalyzing the synthesis of glucosyl-3-phosphoglycerate (GPG) from GDP-glucose and D-3-phosphoglycerate, with a high substrate specificity. The recombinant MpgP protein dephosphorylated GPG to GG and was also able to dephosphorylate mannosyl-3-phosphoglycerate (MPG) but no other substrate tested. Similar flexibilities in substrate specificity were confirmed in vitro for the MpgPs from Thermus thermophilus, Pyrococcus horikoshii, and "Dehalococcoides ethenogenes." GpgS had maximal activity at 50°C. The maximal activity of GpgP was at 50°C with GPG as the substrate and at 60°C with MPG. Despite the similarity of the sugar donors GDP-glucose and GDP-mannose, the enzymes for the synthesis of GPG or MPG share no amino acid sequence identity, save for short motifs. However, the hydrolysis of GPG and MPG is carried out by phosphatases encoded by homologous genes and capable of using both substrates. To our knowledge, this is the first report of the elucidation of a biosynthetic pathway for glucosylglycerate.Most microorganisms capable of osmotic adjustment accumulate low-molecular-weight organic compounds, commonly designated compatible solutes, which can be taken up from the environment or synthesized de novo (6). Although the uptake of organic solutes such as glycine betaine and trehalose, among others, by microorganisms under salt stress is preferred because it is energetically favorable (10), many organisms synthesize specific compatible solutes because these are not present in the environment or those that are present do not fulfill the specific requirements of the organisms.Ectoine, glycine betaine, trehalose, and glutamate are among the most common compatible solutes of bacteria and archaea, where they normally accumulate in response to stress imposed by salt (10). Mannosylglycerate (MG), di-myo-inositol-phosphate, and diglycerol-phosphate have a more restricted distribution, being found primarily in (hyper)thermophilic prokaryotes. Mannosylglycerate is widespread in (hyper)thermophilic bacteria and archaea and is also found in some red algae (21, 35). Cyclic 2,3-bisphosphoglycerate has only been encountered in methanogens (20,25,36).The rare solute glucosylglycerate (GG) was originally identified in the cyanobacterium Agmenellum quadruplicatum strain PCC7002 grown under nitrogen-limiting conditions (22). This solute was also detected in the archaeon Methanohalophilus portucalensis strain FDF...

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LOW MOLECULAR WEIGHT CARBOHYDRATES OF THE BANGIOPHYCIDAE (RHODOPHYTA)¹

Cited by 61 publications

References 15 publications

Compatible Solutes of the HyperthermophilePalaeococcus ferrophilus: Osmoadaptation and Thermoadaptation in the OrderThermococcales

Compatible Solutes of the HyperthermophilePalaeococcus ferrophilus: Osmoadaptation and Thermoadaptation in the OrderThermococcales

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

Characterization of the Biosynthetic Pathway of Glucosylglycerate in the Archaeon Methanococcoides burtonii

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LOW MOLECULAR WEIGHT CARBOHYDRATES OF THE BANGIOPHYCIDAE (RHODOPHYTA)1

Cited by 61 publications

References 15 publications

Compatible Solutes of the HyperthermophilePalaeococcus ferrophilus: Osmoadaptation and Thermoadaptation in the OrderThermococcales

Compatible Solutes of the HyperthermophilePalaeococcus ferrophilus: Osmoadaptation and Thermoadaptation in the OrderThermococcales

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

Characterization of the Biosynthetic Pathway of Glucosylglycerate in the Archaeon Methanococcoides burtonii

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LOW MOLECULAR WEIGHT CARBOHYDRATES OF THE BANGIOPHYCIDAE (RHODOPHYTA)¹