Thermococcus celer, isolated from a solfataric marine water hole on a beach of Vulcano, Italy, is a spheric organism of about 1 μm diameter, during multiplication often constricted to diploforms. The organism utilizes peptides and protein, which are oxidized to CO(2) by sulfur respiration. Alternatively, though less efficiently, it can exist by an unknown type of fermentation. The optimal growth temperature is 88 °C, the optimal pH 5.8, the optimal NaCl concentration 3.8 g/l. Under these conditions with yeast extract (2 g/l) as carbon source and in the presence of finely distributed sulfur (10 g/1), the generation time is about 50 min. The envelope consists of subunits in two dimensional hexagonal dense packing. The absence of murein, the presence of polyisopranyl alcohols in the membrane, the component pattern and the rifampicin resistance of the DNA dependent RNA polymerase and the insensitivity of the organism towards the antibiotics streptomycin and vancomycin prove the archaebacterial nature of Thermococcus celer. The component pattern of the DNA dependent RNA polymerase conforms with the type pattern of RNA polymerases from thermoacidophilic archaebacteria. The absence of an immunochemical cross-reaction of the enzyme from Thermococcus with those from Thermoproteus, Desulfurococcus, Sulfolobus and Thermoplasma and the extent of cross-hybridization of the 16S rRNA with DNAs of other thermoacidophiles place it into the thermoacidophilic branch of the archaebacteria as a novel isolated genus.
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http://dx.doi.org/10.1016/S0723-2020(83)80036-8 | DOI Listing |
Nat Commun
April 2022
Shanghai Public Health Clinical Center, State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, Department of Biochemistry and Biophysics, School of Life Sciences, Fudan University, Shanghai, 200438, China.
Besides the canonical RNA-based RNase P, pre-tRNA 5'-end processing can also be catalyzed by protein-only RNase P (PRORP). To date, various PRORPs have been discovered, but the basis underlying substrate binding and cleavage by HARPs (homolog of Aquifex RNase P) remains elusive. Here, we report structural and biochemical studies of HARPs.
View Article and Find Full Text PDFJ Microbiol
April 2020
Korea Institute of Ocean Science and Technology, Busan, 49111, Republic of Korea.
A strictly anaerobic, dissimilatory Fe(III)-reducing hyperthermophilic archaeon, designated as strain IOH1, was isolated from a new deep-sea hydrothermal vent (Onnuri Vent Field) area in the Central Indian Ocean ridge. Strain IOH1 showed > 99% 16S rRNA gene sequence similarity with Thermococcus celericrescens TS2 (99.4%) and T.
View Article and Find Full Text PDFGenome Announc
February 2018
CNRS UMR5240, INSA Lyon, Université de Lyon, Villeurbanne, France
We report here the genome sequences of the type strains of the species , , , , , , , , , and , as well as the prototype of a possible type strain of a novel species, strain P6.
View Article and Find Full Text PDFInt J Syst Evol Microbiol
August 2013
UMR6197, Laboratoire de Microbiologie des Environnements Extrêmes, IUEM, Technopôle Brest-Iroise, F-29280 Plouzané, France.
A novel hyperthermophilic, anaerobic archaeon, strain Bio-pl-0405IT2(T), was isolated from a hydrothermal chimney sample collected from the East Pacific Rise at 2700 m depth in the 'Sarah Spring' area (7° 25' 24" S 107° 47' 66" W). Cells were irregular, motile cocci (0.8-1.
View Article and Find Full Text PDFPLoS One
July 2012
Centre for Protein Science and Crystallography, School of Life Science, The Chinese University of Hong Kong, Hong Kong, China.
Optimization of the surface charges is a promising strategy for increasing thermostability of proteins. Electrostatic contribution of ionizable groups to the protein stability can be estimated from the differences between the pKa values in the folded and unfolded states of a protein. Using this pKa-shift approach, we experimentally measured the electrostatic contribution of all aspartate and glutamate residues to the stability of a thermophilic ribosomal protein L30e from Thermococcus celer.
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