Archaeal molecular chaperones: Protein folding mechanism of the archaeal chaperonin.
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Accession number;03A0040616
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| Title;Archaeal molecular chaperones: Protein folding mechanism of the archaeal chaperonin. |
| Author;
YOSHIDA TAKAO
(Kyoto Univ., Inst. Frontier Medical Sci., JPN)
YODA MASAFUMI
(Tokyo Univ. of Agric. and Technol., Fac. of Technol.)
MARUYAMA TADASHI
(Marine Biotechnology Inst. (MBI), JPN)
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Journal Title;Protein, Nucleic Acid and Enzyme
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Journal Code:F0325A
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ISSN:0039-9450
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VOL.48;NO.1;PAGE.33-39(2003)
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| Figure&Table&Reference;FIG.4, TBL.2, REF.27 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Factors such as molecular chaperones involved in protein folding in archaea become less in numbers when the optimum growth temperature of archaea becomes higher. Especially in super-thermophilic archaea, only 4 protein folding factors have been reported so far, e.g., small HSP, shaperonin, prefoldin, and PPIase. Shaperonin ranked as a representative of archaeal molecular chaperons belongs to a group-2-type shaperonin, and is composed of one to three subunits. Shaperonin from super thermophilic archaebacteria Thermococcus forms a heterooligomer consisted of 2 kinds of subunits. Their subunits' composition changes according to growth temperature,and the mechanisms of their protein folding has been recently clarified. |
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