Nutrient utilization and transport in the thermoacidophilic archaeon Sulfolobus shibatae

Yallop, C.A.; Charalambous, Bambos M.

doi:10.1099/13500872-142-12-3373

Cited by 7 publications

(4 citation statements)

References 33 publications

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“…Similar data were described by Dib et al [17], where most of the isolates from lagoons from Argentinean Puna were able to grow at high arsenic concentration, especially As[III] [17]. Strains isolated from similar environments, Sulfolobus shibatae and Acidithiobacillus caldus, also improved their growth in the presence of As[III], compared to the control medium [51][52][53]. Although the potential mechanisms of arsenic resistance have not been studied in this work, the presence of arsenic resistance genes in microorganisms isolated from lagoons of the Andean Puna has been studied in previous works of our group [20,38,41,54].…”

Section: Effect Of Arsenic On Dm2 and Tc1supporting

confidence: 83%

Haloarchaea from the Andean Puna: Biological Role in the Energy Metabolism of Arsenic

et al. 2018

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Biofilms, microbial mats, and microbialites dwell under highly limiting conditions (high salinity, extreme aridity, pH, and elevated arsenic concentration) in the Andean Puna. Only recent pioneering studies have described the microbial diversity of different Altiplano lakes and revealed their unexpectedly diverse microbial communities. Arsenic metabolism is proposed to be an ancient mechanism to obtain energy by microorganisms. Members of Bacteria and Archaea are able to exploit arsenic as a bioenergetic substrate in either anaerobic arsenate respiration or chemolithotrophic growth on arsenite. Only six aioAB sequences coding for arsenite oxidase and three arrA sequences coding for arsenate reductase from haloarchaea were previously deposited in the NCBI database. However, no experimental data on their expression and function has been reported. Recently, our working group revealed the prevalence of haloarchaea in a red biofilm from Diamante Lake and microbial mat from Tebenquiche Lake using a metagenomics approach. Also, a surprisingly high abundance of genes used for anaerobic arsenate respiration (arr) and arsenite oxidation (aio) was detected in the Diamante's metagenome. In order to study in depth the role of arsenic in these haloarchaeal communities, in this work, we obtained 18 haloarchaea belonging to the Halorubrum genus, tolerant to arsenic. Furthermore, the identification and expression analysis of genes involved in obtaining energy from arsenic compounds (aio and arr) showed that aio and arr partial genes were detected in 11 isolates, and their expression was verified in two selected strains. Better growth of two isolates was obtained in presence of arsenic compared to control. Moreover, one of the isolates was able to oxidize As[III]. The confirmation of the oxidation of arsenic and the transcriptional expression of these genes by RT-PCR strongly support the hypothesis that the arsenic can be used in bioenergetics processes by the microorganisms flourishing in these environments.

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Section: Effect Of Arsenic On Dm2 and Tc1supporting

confidence: 83%

Haloarchaea from the Andean Puna: Biological Role in the Energy Metabolism of Arsenic

et al. 2018

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“…We therefore conclude that the GBP is a subunit of an ABC transport system. The binding-proteindependent maltose/trehalose transporters of Thermococcus litoralis (10) and S. shibatae (27) and the glucose transporter of S. solfataricus exhibit very high affinities for their sugar substrates, i.e., in the submicromolar range. The high affinity of the binding protein allows these archaeal cells to utilize carbon sources efficiently in substrate-poor environments such as the hydrothermal vents in the deep sea or the hot sulfuric pools.…”

Section: Discussionmentioning

confidence: 99%

Glucose Transport in the Extremely Thermoacidophilic Sulfolobus solfataricus Involves a High-Affinity Membrane-Integrated Binding Protein

et al. 1999

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The archaeon Sulfolobus solfataricus grows optimally at 80°C and pH 2.5 to 3.5 on carbon sources such as yeast extracts, tryptone, and various sugars. Cells rapidly accumulate glucose. This transport activity involves a membrane-bound glucose-binding protein that interacts with its substrate with very high affinity (Kd of 0.43 μM) and retains high glucose affinity at very low pH values (as low as pH 0.6). The binding protein was extracted with detergent and purified to homogeneity as a 65-kDa glycoprotein. The gene coding for the binding protein was identified in the S. solfataricus P2 genome by means of the amino-terminal amino acid sequence of the purified protein. Sequence analysis suggests that the protein is anchored to the membrane via an amino-terminal transmembrane segment. Neighboring genes encode two membrane proteins and an ATP-binding subunit that are transcribed in the reverse direction, whereas a homologous gene cluster inPyrococcus horikoshii OT3 was found to be organized in an operon. These data indicate that S. solfataricus utilizes a binding-protein-dependent ATP-binding cassette transporter for the uptake of glucose.

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“…Maltose utilization by these Sulfolobus species necessitates mechanisms for assimilation of maltose or maltodextrins, and specific transport systems have been identified recently in S. shibatae (51). However, the purified S. solfataricus enzyme also uses glycogen as a substrate.…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization of the α-Glucosidase Gene (malA) from the Hyperthermophilic ArchaeonSulfolobus solfataricus

et al. 1998

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Acidic hot springs are colonized by a diversity of hyperthermophilic organisms requiring extremes of temperature and pH for growth. To clarify how carbohydrates are consumed in such locations, the structural gene (malA) encoding the major soluble α-glucosidase (maltase) and flanking sequences fromSulfolobus solfataricus were cloned and characterized. This is the first report of an α-glucosidase gene from the archaeal domain. malA is 2,083 bp and encodes a protein of 693 amino acids with a calculated mass of 80.5 kDa. It is flanked on the 5′ side by an unusual 1-kb intergenic region. Northern blot analysis of themalA region identified transcripts for malA and an upstream open reading frame located 5′ to the 1-kb intergenic region. The malA transcription start site was located by primer extension analysis to a guanine residue 8 bp 5′ of themalA start codon. Gel mobility shift analysis of themalA promoter region suggests that sequences 3′ to position −33, including a consensus archaeal TATA box, play an essential role in malA expression. malA homologs were detected by Southern blot analysis in other S. solfataricus strains and in Sulfolobus shibatae, while no homologs were evident in Sulfolobus acidocaldarius, lending further support to the proposed revision of the genus Sulfolobus. Phylogenetic analyses indicate that the closest S. solfataricusα-glucosidase homologs are of mammalian origin. Characterization of the recombinant enzyme purified from Escherichia colirevealed differences from the natural enzyme in thermostability and electrophoretic behavior. Glycogen is a substrate for the recombinant enzyme. Unlike maltose hydrolysis, glycogen hydrolysis is optimal at the intracellular pH of the organism. These results indicate a unique role for the S. solfataricus α-glucosidase in carbohydrate metabolism.

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Nutrient utilization and transport in the thermoacidophilic archaeon Sulfolobus shibatae

Cited by 7 publications

References 33 publications

Haloarchaea from the Andean Puna: Biological Role in the Energy Metabolism of Arsenic

Haloarchaea from the Andean Puna: Biological Role in the Energy Metabolism of Arsenic

Glucose Transport in the Extremely Thermoacidophilic Sulfolobus solfataricus Involves a High-Affinity Membrane-Integrated Binding Protein

Molecular Characterization of the α-Glucosidase Gene (malA) from the Hyperthermophilic ArchaeonSulfolobus solfataricus

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