Activity and Transcriptional Regulation of Bacterial Protein-Like Glycerol-3-Phosphate Dehydrogenase of the Haloarchaea in Haloferax volcanii

Rawls, Katherine S.; Martin, Jonathan H.; Maupin-Furlow, Julie A.

doi:10.1128/jb.06126-11

Cited by 9 publications

(13 citation statements)

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“…The oxidation of G3P to DHAP by heterotrimeric G3PDH (GlpABC; ‘anaerobic G3P dehydrogenase’), a membrane‐associated enzyme, is coupled to the reduction of fumarate or nitrate, with concomitant translocation of protons to generate a proton motive force (Kistler and Lin, ; Ingledew and Poole, ). The presence of a BFD‐like domain suggests this protein may serve as a general redox enzyme and/or in iron metabolism in addition to G3P oxidation (Garg et al ., ; Rawls et al ., ).…”

Section: G3pdh (Ec 1153)mentioning

confidence: 97%

“…In Hfx. volcanii , GlpABC functions during aerobic growth on glycerol, and the genes are cotranscribed (Sherwood et al ., ; Rawls et al ., ). The Hfx.…”

Section: G3pdh (Ec 1153)mentioning

confidence: 97%

“…Analysis of Hfx. volcanii knockout strains revealed that only one copy (the glpABC located next to glpK on the primary replicon) is required for growth on glycerol (Rawls et al ., ). The levels of transcripts for glpABC and glpK were significantly upregulated in aerated cultures in the presence of glycerol (Sherwood et al ., ).…”

Section: G3pdh (Ec 1153)mentioning

confidence: 97%

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Glycerol metabolism of haloarchaea

Williams

Allen

Tschitschko

et al. 2016

Environmental Microbiology

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Summary Haloarchaea are heterotrophic members of the Archaea that thrive in hypersaline environments, often feeding off the glycerol that is produced as an osmolyte by eucaryotic Dunaliella during primary production. In this study we analyzed glycerol metabolism genes in closed genomes of haloarchaea and examined published data describing the growth properties of haloarchaea and experimental data for the enzymes involved. By integrating the genomic data with knowledge from the literature, we derived an understanding of the ecophysiology and evolutionary properties of glycerol catabolic pathways in haloarchaea.

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Section: G3pdh (Ec 1153)mentioning

confidence: 97%

“…In Hfx. volcanii , GlpABC functions during aerobic growth on glycerol, and the genes are cotranscribed (Sherwood et al ., ; Rawls et al ., ). The Hfx.…”

Section: G3pdh (Ec 1153)mentioning

confidence: 97%

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Glycerol metabolism of haloarchaea

Williams

Allen

Tschitschko

et al. 2016

Environmental Microbiology

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“…Halorhabdus tiamatea has all genes for anaerobic glycerol degradation: a glycerol kinase and an anaerobic glycerol-3-phosphate dehydrogenase (glpABC) (Rawls et al, 2011). In Escherichia coli, the anaerobic oxidation of glycerol-3-phosphate to dihydroxyacetone phosphate by GlpABC is coupled to the reduction of fumarate to succinate (Schryvers and Weiner, 1981), but other halophilic archaea such as representatives of the genera Haloferax and Haloarcula have been shown to metabolize glycerol under anoxic conditions to D-lactate, acetate and pyruvate (Oren and Gurevich, 1994).…”

Section: Fermentationsmentioning

confidence: 99%

Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements identify the first cultivated euryarchaeon from a deep‐sea anoxic brine lake as potential polysaccharide degrader

Werner

Ferrer

Michel

et al. 2014

Environmental Microbiology

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Euryarchaea from the genus Halorhabdus have been found in hypersaline habitats worldwide, yet are represented by only two isolates: Halorhabdus utahensis AX-2T from the shallow Great Salt Lake of Utah, and Halorhabdus tiamatea SARL4BT from the Shaban deep-sea hypersaline anoxic lake (DHAL) in the Red Sea. We sequenced the H. tiamatea genome to elucidate its niche adaptations. Among sequenced archaea, H. tiamatea features the highest number of glycoside hydrolases, the majority of which were expressed in proteome experiments. Annotations and glycosidase activity measurements suggested an adaptation towards recalcitrant algal and plant-derived hemicelluloses. Glycosidase activities were higher at 2% than at 0% or 5% oxygen, supporting a preference for low-oxygen conditions. Likewise, proteomics indicated quinone-mediated electron transport at 2% oxygen, but a notable stress response at 5% oxygen. Halorhabdus tiamatea furthermore encodes proteins characteristic for thermophiles and light-dependent enzymes (e.g. bacteriorhodopsin), suggesting that H. tiamatea evolution was mostly not governed by a cold, dark, anoxic deep-sea habitat. Using enrichment and metagenomics, we could demonstrate presence of similar glycoside hydrolase-rich Halorhabdus members in the Mediterranean DHAL Medee, which supports that Halorhabdus species can occupy a distinct niche as polysaccharide degraders in hypersaline environments.

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“…The enzymes activities were measured directly after the preparation of cell‐free extracts. The specific activities of glycerol‐3‐phosphate dehydrogenase, DHA kinase, glycerol dehydrogenase, and glycerol kinase were determined as described elsewhere (Hayashi & Lin, ; Norbeck & Blomberg, ; Rawls, Martin, & Maupin‐Furlow, ; Yamada, Nagao, Nishise, & Tani, ). Experiments were performed at least twice.…”

Section: Methodsmentioning

confidence: 99%

Overexpression of the genes of glycerol catabolism and glycerol facilitator improves glycerol conversion to ethanol in the methylotrophic thermotolerant yeast Ogataea polymorpha

Semkiv

Kata

Ternavska

et al. 2019

Yeast

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Production of fuel ethanol is one of the possible ways to utilize crude glycerol, substantial amounts of which are produced by biodiesel industry. Earlier, we have described construction of the recombinant strains of methylotrophic thermotolerant yeast Ogataea polymorpha with simultaneous overexpression of the genes PDC1and ADH1, which produced increased amounts of ethanol from glycerol. In this work, we have further improved these strains by overexpression of genes involved either in oxidative (through dihydroxyacetone) or phosphorylative (through glycerol-3-phosphate) pathway of glycerol catabolism, as well as heterologous gene coding for glycerol transporter FPS1 from Komagataella phaffii (formerly, Pichia pastoris).Obtained recombinant strains produced up to 10.7 g/L of ethanol (with ethanol productivity 30 mg/g of biomass/hr and yield 132 mg/g of consumed glycerol) from pure glycerol and up to 3.55 g/L of ethanol (with ethanol productivity 11.6 mg/g of biomass/hr and yield 72.3 mg/g of consumed glycerol) from crude glycerol as a carbon source, which is approximately 15 times more relative to that of the O. polymorpha wild-type strain and 2.2 more relative to the earlier constructed strain.

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Activity and Transcriptional Regulation of Bacterial Protein-Like Glycerol-3-Phosphate Dehydrogenase of the Haloarchaea in Haloferax volcanii

Cited by 9 publications

References 0 publications

Glycerol metabolism of haloarchaea

Glycerol metabolism of haloarchaea

Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements identify the first cultivated euryarchaeon from a deep‐sea anoxic brine lake as potential polysaccharide degrader

Overexpression of the genes of glycerol catabolism and glycerol facilitator improves glycerol conversion to ethanol in the methylotrophic thermotolerant yeast Ogataea polymorpha

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