Choline-O-Sulfate Biosynthesis in Plants (Identification and Partial Characterization of a Salinity-Inducible Choline Sulfotransferase from Species of Limonium (Plumbaginaceae)

Rivoal, Jean; Hanson, Andrew D.

doi:10.1104/pp.106.3.1187

Cited by 34 publications

(18 citation statements)

References 28 publications

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“…This degradative pathway is largely present on genome 4E, whereas glycine degradation was encoded in all three phylotypes. As choline-O-sulfate is synthesized by different microorganisms (Spencer and Harada, 1960;Fitzgerald and Luschinski, 1977;Rivoal and Hanson, 1994), it is likely available as carbon and sulfur substrate for Poribacteria.…”

Section: Sulfatasesmentioning

confidence: 99%

Single-cell genomics reveals complex carbohydrate degradation patterns in poribacterial symbionts of marine sponges

et al. 2013

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Many marine sponges are hosts to dense and phylogenetically diverse microbial communities that are located in the extracellular matrix of the animal. The candidate phylum Poribacteria is a predominant member of the sponge microbiome and its representatives are nearly exclusively found in sponges. Here we used single-cell genomics to obtain comprehensive insights into the metabolic potential of individual poribacterial cells representing three distinct phylogenetic groups within Poribacteria. Genome sizes were up to 5.4 Mbp and genome coverage was as high as 98.5%. Common features of the poribacterial genomes indicated that heterotrophy is likely to be of importance for this bacterial candidate phylum. Carbohydrate-active enzyme database screening and further detailed analysis of carbohydrate metabolism suggested the ability to degrade diverse carbohydrate sources likely originating from seawater and from the host itself. The presence of uronic acid degradation pathways as well as several specific sulfatases provides strong support that Poribacteria degrade glycosaminoglycan chains of proteoglycans, which are important components of the sponge host matrix. Dominant glycoside hydrolase families further suggest degradation of other glycoproteins in the host matrix. We therefore propose that Poribacteria are well adapted to an existence in the sponge extracellular matrix. Poribacteria may be viewed as efficient scavengers and recyclers of a particular suite of carbon compounds that are unique to sponges as microbial ecosystems.

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Section: Sulfatasesmentioning

confidence: 99%

Single-cell genomics reveals complex carbohydrate degradation patterns in poribacterial symbionts of marine sponges

et al. 2013

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“…The conversion of choline to choline-O-sulfate is catalyzed by a 3Ј-phosphoadenosine-5Ј-phosphosulfate-dependent choline sulfotransferase (Fig. 3) (Rivoal and Hanson, 1994). This sulfotransferase is a soluble enzyme with an extremely high affinity for choline (K m ϭ 5.5 m), which probably reflects the low cytoplasmic choline levels that prevail in plants (Nuccio et al, 1998).…”

Section: Choline-o-sulfatementioning

confidence: 99%

“…This sulfotransferase is a soluble enzyme with an extremely high affinity for choline (K m ϭ 5.5 m), which probably reflects the low cytoplasmic choline levels that prevail in plants (Nuccio et al, 1998). Saline conditions induce sulfotransferase enzyme activity in both leaves and roots (Rivoal and Hanson, 1994).…”

Section: Choline-o-sulfatementioning

confidence: 99%

Betaines and Related Osmoprotectants. Targets for Metabolic Engineering of Stress Resistance1

1999

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“…One host-derived molecule that is important in a number of bacterium-host interactions is the quaternary amine alcohol choline. Choline is present on and around eukaryotes in its free form (10,23), as a moiety on the soluble molecules choline-O-phosphate and choline-O-sulfate (13,31), and as the head group moiety on sphingomyelin and phosphatidylcholine (46). Catabolism of host-derived choline is important in many bacteria for generation of the osmoprotectant glycine betaine (GB), which has been linked to enhanced bacterial survival in high-salinity environments (4,22).…”

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confidence: 99%

Small-Molecule Inhibition of Choline Catabolism in Pseudomonas aeruginosa and Other Aerobic Choline-Catabolizing Bacteria

Fitzsimmons

Flemer

Wurthmann

et al. 2011

Appl Environ Microbiol

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Choline is abundant in association with eukaryotes and plays roles in osmoprotection, thermoprotection, and membrane biosynthesis in many bacteria. Aerobic catabolism of choline is widespread among soil proteobacteria, particularly those associated with eukaryotes. Catabolism of choline as a carbon, nitrogen, and/or energy source may play important roles in association with eukaryotes, including pathogenesis, symbioses, and nutrient cycling. We sought to generate choline analogues to study bacterial choline catabolism in vitro and in situ. Here we report the characterization of a choline analogue, propargylcholine, which inhibits choline catabolism at the level of Dgc enzyme-catalyzed dimethylglycine demethylation in Pseudomonas aeruginosa. We used genetic analyses and 13 C nuclear magnetic resonance to demonstrate that propargylcholine is catabolized to its inhibitory form, propargylmethylglycine. Chemically synthesized propargylmethylglycine was also an inhibitor of growth on choline. Bioinformatic analysis suggests that there are genes encoding DgcA homologues in a variety of proteobacteria. We examined the broader utility of propargylcholine and propargylmethylglycine by assessing growth of other members of the proteobacteria that are known to grow on choline and possess putative DgcA homologues. Propargylcholine showed utility as a growth inhibitor in P. aeruginosa but did not inhibit growth in other proteobacteria tested. In contrast, propargylmethylglycine was able to inhibit cholinedependent growth in all tested proteobacteria, including Pseudomonas mendocina, Pseudomonas fluorescens, Pseudomonas putida, Burkholderia cepacia, Burkholderia ambifaria, and Sinorhizobium meliloti. We predict that chemical inhibitors of choline catabolism will be useful for studying this pathway in clinical and environmental isolates and could be a useful tool to study proteobacterial choline catabolism in situ.

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Choline-O-Sulfate Biosynthesis in Plants (Identification and Partial Characterization of a Salinity-Inducible Choline Sulfotransferase from Species of Limonium (Plumbaginaceae)

Cited by 34 publications

References 28 publications

Single-cell genomics reveals complex carbohydrate degradation patterns in poribacterial symbionts of marine sponges

Single-cell genomics reveals complex carbohydrate degradation patterns in poribacterial symbionts of marine sponges

Betaines and Related Osmoprotectants. Targets for Metabolic Engineering of Stress Resistance1

Small-Molecule Inhibition of Choline Catabolism in Pseudomonas aeruginosa and Other Aerobic Choline-Catabolizing Bacteria

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