title: Stimulated interaction between  and  subunits of tryptophan synthase from hyperthermophile enhances its thermal stability.
abstract: Tryptophan synthase from hyperthermophile, Pyrococcus furiosus, was found to be a tetrameric form (22) composed of and 2 subunits. To elucidate the relationship between the features of the subunit association and the thermal stability of the tryptophan synthase, the subunit association and thermal stability were examined by isothermal titration calorimetry and differential scanning calorimetry, respectively, in comparison with those of the counterpart from Escherichia coli. The association constants between the and subunits in the hyperthermophile protein were of the order of 108 M1, which were higher by two orders of magnitude than those in the mesophile one. The negative values of the heat capacity change and enthalpy change upon the subunit association were much lower in the hyperthermophile protein than in the mesophile one, indicating that the conformational change of the hyperthermophile protein coupled to the subunit association is slight. The denaturation temperature of the subunit from the hyperthermophile was enhanced by 17 degrees C due to the formation of the 22 complex. This increment in denaturation temperature due to complex formation could be quantitatively estimated by the increase in the association constant compared with that of the counterpart from E. coli.
authors.affiliation: Institute for Protein Research, Osaka University, Suita City, Osaka 565-0871, Japan.
authors.forename: Kyoko
authors.initials: K
authors.lastname: Ogasahara
authors.forename: Masami
authors.initials: M
authors.lastname: Ishida
authors.forename: Katsuhide
authors.initials: K
authors.lastname: Yutani
mesh_terms: D000595:Amino Acid Sequence; D055592:Biophysical Phenomena; D001703:Biophysics; D002151:Calorimetry; D002152:Calorimetry, Differential Scanning; D004926:Escherichia coli / Q000201:enzymology; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D011485:Protein Binding; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D020027:Pyrococcus furiosus / Q000201:enzymology; D011994:Recombinant Proteins / Q000737:chemistry; D013696:Temperature; D013997:Time Factors; D014367:Tryptophan Synthase / Q000737:chemistry* / Q000378:metabolism; D014461:Ultracentrifugation
chemical_list: D011994:Recombinant Proteins; D014367:Tryptophan Synthase