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Schlagwörter:
Chaperonin; Groel; Tcp1; Thermoplasma acidophilum; Thermosome.; T-complex polypeptide-1; Molecular chaperone; Thermophilic archaebacterium; Heat-shock; Proteins; Subunits; Tubulin; Plant; Cell; Gene.; Biochemistry & biophysics.
Zusammenfassung:
The thermosome, a chaperonin from the archaebacterium Thermoplasma acidophilum, consists of two subunits (M(r) 58 000 and 60 000) which assemble into a cylindrical complex of pseudo eight-fold rotational symmetry. The sequences of the two subunits are approximately 60 % identical to each other and to TF55 from Sulfolobus shibatae, and are 30-40% identical to the subunits of the TCP1 containing ring complex (TRiC) from the eukaryotic cytosol. A dendrogram of this family of chaperonins contains eight eukaryotic branches of TRiC subunits and one archaebacterial branch of thermosome subunits. Alignment of thermosome/TRiC sequences with eubacterial and eukaryotic Hsp60 sequences reveals a statistically significant similarity in two large N- and C-terminal blocks of sequence. Based on this alignment and on the recently published crystal structure of GroEL, we propose that subunits of the thermosome/TRiC family of chaperonins have a similar equatorial domain and overall domain topology as GroEL but differ in the structure of the apical domain. [References: 42]
