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Hyperthermophilic Organisms (hyperthermophilic + organism)
Selected AbstractsCompatible solutes of organisms that live in hot saline environmentsENVIRONMENTAL MICROBIOLOGY, Issue 9 2002Helena Santos Summary The accumulation of organic solutes is a prerequisite for osmotic adjustment of all microorganisms. Thermophilic and hyperthermophilic organisms generally accumulate very unusual compatible solutes namely, di- myo -inositol-phosphate, di-mannosyl-di- myo -inositol-phosphate, di-glycerol-phosphate, mannosylglycerate and mannosylglyceramide, which have not been identified in bacteria or archaea that grow at low and moderate temperatures. There is also a growing awareness that some of these compatible solutes may have a role in the protection of cell components against thermal denaturation. Mannosylglycerate and di-glycerol-phosphate have been shown to protect enzymes and proteins from thermal denaturation in vitro as well, or better, than compatible solutes from mesophiles. The pathways leading to the synthesis of some of these compatible solutes from thermophiles and hyperthermophiles have been elucidated. However, large numbers of questions remain unanswered. Fundamental and applied interest in compatible solutes and osmotic adjustment in these organisms, drives research that, will, in the near future, allow us to understand the role of compatible solutes in osmotic protection and thermoprotection of some of the most fascinating organisms known on Earth. [source] Biotinylation in the hyperthermophile Aquifex aeolicusFEBS JOURNAL, Issue 6 2003Isolation of a cross-linked BPL:BCCP complex Biotin protein ligase (BPL) catalyses the biotinylation of the biotin carboxyl carrier protein (BCCP) subunit of acetyl CoA carboxylase and this post-translational modification of a single lysine residue is exceptionally specific. The exact details of the protein,protein interactions involved are unclear as a BPL:BCCP complex has not yet been isolated. Moreover, detailed information is lacking on the composition, biosynthesis and role of fatty acids in hyperthermophilic organisms. We have cloned, overexpressed and purified recombinant BPL and the biotinyl domain of BCCP (BCCP,67) from the extreme hyperthermophile Aquifex aeolicus. In vitro assays have demonstrated that BPL catalyses biotinylation of lysine 117 on BCCP,67 at temperatures of up to 70 °C. Limited proteolysis of BPL with trypsin and chymotrypsin revealed a single protease-sensitive site located 44 residues from the N-terminus. This site is adjacent to the predicted substrate-binding site and proteolysis of BPL is significantly reduced in the presence of MgATP and biotin. Chemical crosslinking with 1-ethyl-3-(dimethylamino-propyl)-carbodiimide (EDC) allowed the isolation of a BPL:apo-BCCP,67 complex. Furthermore, this complex was also formed between BPL and a BCCP,67 mutant lacking the lysine residue (BCCP,67 K117L) however, complex formation was considerably reduced using holo-BCCP,67. These observations provide evidence that addition of the biotin prosthetic group reduces the ability of BCCP,67 to heterodimerize with BPL, and emphasizes that a network of interactions between residues on both proteins mediates protein recognition. [source] Characterisation of Heterotrophic Microorganisms Isolated form the "Grotta Azzura" of Cape Palinuro (Salerno, Italy)MARINE ECOLOGY, Issue 2002Francesco Canganella Abstract. Hydrothermal vent ecosystems have been extensively investigated during the last 20 years; shallow water hot springs (typically found below 50 m depth) have also been studied, and from these ecosystems many thermophilic and hyperthermophilic organisms were isolated and described. The submarine caves of Cape Palinuro were discovered long ago, but only during the last decades were geological and biological investigations carried out, yielding a large number of reports on this fascinating environment. During the last two years, several samples of water, mud, and/or bacterial mat were collected within the "Grotta Azzurra", and enrichment experiments were performed using peptone, starch, glucose or pullulan as main organic nutrients. Many heterotrophic strains were isolated and most of them grew optimally between 37 and 43 ° C with the addition of 0-2 % NaCl. Growth was usually observed between 10 and 50 ° C the range of growth pH was 4 to 9, and NaCl concentrations up to 10,12 % were tolerated in most cases. The analysis of 16S rDNA performed with the most representative isolates showed a close phylogenetic relationship with the genera Bacillus, Vibrio, Citrobacter and Escherichia. Moreover, an isolate showing morphological and physiological similarities with the genus Enterococcus was characterised and taxonomically described based on the 16S rDNA sequence. [source] Crystallization and preliminary X-ray analysis of mannosyl-3-phosphoglycerate synthase from Thermus thermophilus HB27ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 10 2009Susana Gonçalves Mannosylglycerate (MG) is a compatible solute that is widespread in marine organisms that are adapted to hot environments, with its intracellular pool generally increasing in response to osmotic stress. These observations suggest that MG plays a relevant role in osmoadaptation and thermoadaptation. The pathways for the synthesis of MG have been characterized in a number of thermophilic and hyperthermophilic organisms. Mannosyl-3-phosphoglycerate synthase (MpgS) is a key enzyme in the biosynthesis of MG. Here, the purification, crystallization and preliminary crystallographic characterization of apo MpgS from Thermus thermophilus HB27 are reported. The addition of Zn2+ to the crystallization buffer was essential in order to obtain crystals. The crystals belonged to one of the enantiomorphic tetragonal space groups P41212 or P43212, with unit-cell parameters a = b = 113, c = 197,Å. Diffraction data were obtained to a resolution of 2.97,Å. [source] | |||||||||||||