title: Molecular bases of thermophily in hyperthermophiles.
abstract: I reflect on some of our studies on the hyperthermophilic archaeon, Thermococcus kodakarensis KOD1 and its enzymes. The strain can grow at temperatures up to 100 °C, and also represents one of the simplest forms of life. As expected, all enzymes, DNA, RNA, cytoplasmic membrane, and cytoplasmic solute displayed remarkable thermostability, and we have determined some of the basic principles that govern this feature. To our delight, many of the enzymes exhibited unique biochemical properties and novel structures not found in mesophilic proteins. Here, I will focus on some enzymes whose three-dimensional structures are characteristic of thermostable enzymes. I will also add some examples on the stabilization of DNA, RNA, cytoplasmic membrane, and cytoplasmic solute.
authors.affiliation: Department of Biotechnology, Ritsumeikan University, Shiga, Japan. imanaka@sk.ritsumei.ac.jp
authors.forename: Tadayuki
authors.initials: T
authors.lastname: Imanaka
mesh_terms: D001105:Archaea / Q000166:cytology / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D004247:DNA / Q000737:chemistry; D004795:Enzyme Stability; D006358:Hot Temperature; D012313:RNA / Q000737:chemistry
chemical_list: D019843:Archaeal Proteins; D012313:RNA; D004247:DNA
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