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The thermosome: archetype of group II chaperonins
Author(s) -
Klumpp Martin,
Baumeister Wolfgang
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00541-9
Subject(s) - chaperonin , groel , groes , subfamily , protein folding , archaea , biology , folding (dsp implementation) , chaperone (clinical) , crystallography , chemistry , biophysics , microbiology and biotechnology , biochemistry , genetics , bacteria , escherichia coli , engineering , electrical engineering , gene , medicine , pathology
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.