scholarly journals Provirus Induction in Hyperthermophilic Archaea: Characterization of Aeropyrum pernix Spindle-Shaped Virus 1 and Aeropyrum pernix Ovoid Virus 1

2011 ◽  
Vol 193 (19) ◽  
pp. 5412-5419 ◽  
Author(s):  
T. Mochizuki ◽  
Y. Sako ◽  
D. Prangishvili
Keyword(s):  
Hyperthermophilic Archaea ◽  
Aeropyrum Pernix

Characterization of a novel moderate-substrate specificity amino acid racemase from the hyperthermophilic archaeon Thermococcus litoralis

2021 ◽  
Author(s):  
Ryushi Kawakami ◽  
Chinatsu Kinoshita ◽  
Tomoki Kawase ◽  
Mikio Sato ◽  
Junji Hayashi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Substrate Specificity ◽  
Enzyme Stability ◽  
Hyperthermophilic Archaea ◽  
Thermococcus Litoralis ◽  
Hyperthermophilic Archaeon ◽  
Aminobutyrate Aminotransferase ◽  
Chaperone Protein ◽  
Amino Acid Racemase

Abstract The amino acid sequence of the OCC_10945 gene product from the hyperthermophilic archaeon Thermococcus litoralis DSM5473, originally annotated as γ-aminobutyrate aminotransferase, is highly similar to that of the uncharacterized pyridoxal 5ʹ-phosphate (PLP)-dependent amino acid racemase from Pyrococcus horikoshii. The OCC_10945 enzyme was successfully overexpressed in Escherichia coli by co-expression with a chaperone protein. The purified enzyme demonstrated PLP-dependent amino acid racemase activity primarily toward Met and Leu. Although PLP contributed to enzyme stability, it only loosely bound to this enzyme. Enzyme activity was strongly inhibited by several metal ions, including Co2+ and Zn2+, and non-substrate amino acids such as l-Arg and l-Lys. These results suggest that the underlying PLP-binding and substrate recognition mechanisms in this enzyme are significantly different from those of the other archaeal and bacterial amino acid racemases. This is the first description of a novel PLP-dependent amino acid racemase with moderate substrate specificity in hyperthermophilic archaea.

scholarly journals Recognition of tRNA by aminoacyl-tRNA synthetase from hyperthermophilic archaea, Aeropyrum pernix K1

2001 ◽  
Vol 1 (1) ◽  
pp. 117-118 ◽  
Author(s):  
J. Yokozawa ◽  
Y. Nagaoka ◽  
T. Umehara ◽  
J. Iwaki ◽  
Y. Kawarabayasi ◽  
...  
Keyword(s):  
Trna Synthetase ◽  
Hyperthermophilic Archaea ◽  
Aminoacyl Trna Synthetase ◽  
Aeropyrum Pernix

scholarly journals Molybdenum-Containing Arsenite Oxidase of the Chemolithoautotrophic Arsenite Oxidizer NT-26

2004 ◽  
Vol 186 (6) ◽  
pp. 1614-1619 ◽  
Author(s):  
Joanne M. Santini ◽  
Rachel N. vanden Hoven
Keyword(s):  
Secretory Pathway ◽  
Alcaligenes Faecalis ◽  
Sequence Analyses ◽  
Arsenite Oxidase ◽  
Sulfolobus Tokodaii ◽  
Aeropyrum Pernix ◽  
Native Molecular Mass ◽  
Iron Sulfur ◽  
Dimethyl Sulfoxide Reductase

ABSTRACT The chemolithoautotroph NT-26 oxidizes arsenite to arsenate by using a periplasmic arsenite oxidase. Purification and preliminary characterization of the enzyme revealed that it (i) contains two heterologous subunits, AroA (98 kDa) and AroB (14 kDa); (ii) has a native molecular mass of 219 kDa, suggesting an α2β2 configuration; and (iii) contains two molybdenum and 9 or 10 iron atoms per α2β2 unit. The genes that encode the enzyme have been cloned and sequenced. Sequence analyses revealed similarities to the arsenite oxidase of Alcaligenes faecalis, the putative arsenite oxidase of the beta-proteobacterium ULPAs1, and putative proteins of Aeropyrum pernix, Sulfolobus tokodaii, and Chloroflexus aurantiacus. Interestingly, the AroA subunit was found to be similar to the molybdenum-containing subunits of enzymes in the dimethyl sulfoxide reductase family, whereas the AroB subunit was found to be similar to the Rieske iron-sulfur proteins of cytochrome bc 1 and b 6 f complexes. The NT-26 arsenite oxidase is probably exported to the periplasm via the Tat secretory pathway, with the AroB leader sequence used for export. Confirmation that NT-26 obtains energy from the oxidation of arsenite was obtained, as an aroA mutant was unable to grow chemolithoautotrophically with arsenite. This mutant could grow heterotrophically in the presence of arsenite; however, the arsenite was not oxidized to arsenate.

scholarly journals Characterization of a Whole Set of tRNA Molecules in an Aerobic Hyper-thermophilic Crenarchaeon, Aeropyrum pernix K1

DNA Research ◽  
2006 ◽  
Vol 12 (6) ◽  
pp. 403-416 ◽  
Author(s):  
S. Yamazaki ◽  
H. Kikuchi ◽  
Y. Kawarabayasi
Keyword(s):  
Aeropyrum Pernix

scholarly journals Physiological and Genomic Characterization of a Hyperthermophilic Archaeon Archaeoglobus neptunius sp. nov. Isolated From a Deep-Sea Hydrothermal Vent Warrants the Reclassification of the Genus Archaeoglobus

2021 ◽  
Vol 12 ◽  
Author(s):  
Galina Slobodkina ◽  
Maxime Allioux ◽  
Alexander Merkel ◽  
Marie-Anne Cambon-Bonavita ◽  
Karine Alain ◽  
...  
Keyword(s):  
Deep Sea ◽  
Hydrothermal Vent ◽  
Single Copy ◽  
Amino Acid Identity ◽  
Hyperthermophilic Archaea ◽  
The Novel ◽  
Flagellar Motility ◽  
Isolation And Characterization ◽  
Mid Atlantic Ridge

Hyperthermophilic archaea of the genus Archaeoglobus are the subject of many fundamental and biotechnological researches. Despite their significance, the class Archaeoglobi is currently represented by only eight species obtained as axenic cultures and taxonomically characterized. Here, we report the isolation and characterization of a new species of Archaeoglobus from a deep-sea hydrothermal vent (Mid-Atlantic Ridge, TAG) for which the name Archaeoglobus neptunius sp. nov. is proposed. The type strain is SE56T (=DSM 110954T = VKM B-3474T). The cells of the novel isolate are motile irregular cocci growing at 50–85°C, pH 5.5–7.5, and NaCl concentrations of 1.5–4.5% (w/v). Strain SE56T grows lithoautotrophically with H2 as an electron donor, sulfite or thiosulfate as an electron acceptor, and CO2/HCO3− as a carbon source. It is also capable of chemoorganotrophic growth by reduction of sulfate, sulfite, or thiosulfate. The genome of the new isolate consists of a 2,115,826 bp chromosome with an overall G + C content of 46.0 mol%. The whole-genome annotation confirms the key metabolic features of the novel isolate demonstrated experimentally. Genome contains a complete set of genes involved in CO2 fixation via reductive acetyl-CoA pathway, gluconeogenesis, hydrogen and fatty acids oxidation, sulfate reduction, and flagellar motility. The phylogenomic reconstruction based on 122 conserved single-copy archaeal proteins supported by average nucleotide identity (ANI), average amino acid identity (AAI), and alignment fraction (AF) values, indicates a polyphyletic origin of the species currently included into the genus Archaeoglobus, warranting its reclassification.

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