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Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP
Author(s) -
Makino Yoshihide,
Taguchi Hideki,
Yoshida Masasuke
Publication year - 1993
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 - 10.1016/0014-5793(93)80838-l
Subject(s) - groel , groes , chaperonin , rhodanese , foldase , protein folding , folding (dsp implementation) , oligomer , biochemistry , proteolysis , biophysics , escherichia coli , chemistry , biology , enzyme , organic chemistry , electrical engineering , gene , engineering
Similar to chaperonins from other sources, intact chaperonin from Escherichia coli (GroEL) exists as a tetradecamer, and the ability to promote folding of other proteins has been considered to be dependent on this oligomeric structure. However, the peptide fragments of GroEL of molecular size 34–50 kDa, which are produced by limited proteolysis of monomeric GroEL and are unable to assemble into an oligomer, retain the ability to promote folding of rhodanese even though the yield of productive folding is lower than the intact GroEL/GroES/ATP system. This promotion by truncated GroEL obeys rapid kinetics and does not require GroES and ATP.