ausblenden:
Schlagwörter:
Protein folding; Chaperone; Tric/cct; Archaeon.; Archaeon sulfolobus-solfataricus; T-complex polypeptide-1; Cytoplasmic chaperonin; Molecular chaperone; Eukaryotic cytosol; Structural characterization; Binding domains; Beta-actin; Heat-shock; In-vitro.; Biochemistry & biophysics.
Zusammenfassung:
The thermosome, the chaperonin of the archaea, and its homologue from the cytosol of eukaryotes, known as TRiC or CCT, form a distinct subfamily of the chaperonins that does not depend on a co-chaperonin for protein folding activity. Recent structural data obtained by cryo- electron microscopy and X-ray crystallography provide the first insights into a novel mechanism remarkably different from that of the bacterial GroEL-GroES system. (C) 1998 Federation of European Biochemical Societies. [References: 49]
