Refolding of proteins by hexadecamers and monomers of the α and β subunits of group II chaperonin from the hyperthermophilic archaeum Thermococcus strain KS-1
In: Biochemical engineering journal, Jg. 18 (2004), Heft 1, S. 73-79
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Zugriff:
The a and β subunits of group II chaperonin from a hyperthermophilic archaeum, Thermococcus strain KS-I, were produced in Escherichia coli. Thermococcus KS-1 α and β chaperonins were purified from a crude cell extract by heat treatment and subsequent chromatographic purification in the presence and absence of Mg2+ to produce hexadecameric and monomeric form, respectively. The monomeric a and β subunits were able to form homo-hexadecamers in the presence of Mg2+. In the absence of ATP, the a and β homo-hexadecamers arrested the refolding of guanidine hydrochloride-denatured Bacillus stearothermophilus leucine dehydrogenase (LeuDH) and Thermus flavus malate dehydrogenase (MDH), which were released by the addition of ATP at 50-65 °C. In the presence of ATP, the a and β homo-hexadecamers facilitated the refolding of LeuDH and MDH. The a homo-hexadecamer showed greater complex stability and greater ability to facilitate the refolding of enzymes than the β homo-hexadecamer. On the other hand, both the a and β monomers facilitated the refolding of the proteins in the absence of ATP. Thermococcus KS-1 chaperonin homo-hexadecamers and monomers could both therefore be used as molecular tools in biotechnology.
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Refolding of proteins by hexadecamers and monomers of the α and β subunits of group II chaperonin from the hyperthermophilic archaeum Thermococcus strain KS-1
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Autor/in / Beteiligte Person: | KOHDA, Jiro ; YAMADA, Tadanori ; YOSHIDA, Takao ; MARUYAMA, Tadashi ; YOHDA, Masafumi ; FUKUDA, Hideki ; KONDO, Akihiko |
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Zeitschrift: | Biochemical engineering journal, Jg. 18 (2004), Heft 1, S. 73-79 |
Veröffentlichung: | Amsterdam; Lausanne; New York, NY: Elsevier Science, 2004 |
Medientyp: | academicJournal |
Umfang: | print, 32 ref |
ISSN: | 1369-703X (print) |
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