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Characterisation of mutations in GroES that allow GroEL to function as a single ring
Author(s) -
Liu Han,
Kovács Eszter,
Lund Peter A.
Publication year - 2009
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/j.febslet.2009.06.027
Subject(s) - groel , groes , mutant , chaperonin , chaperone (clinical) , allosteric regulation , foldase , biophysics , biology , chemistry , microbiology and biotechnology , biochemistry , protein folding , escherichia coli , receptor , gene , medicine , pathology
The chaperonin GroEL contains two seven‐subunit rings, and allosteric signals between them are required to complete the GroEL reaction cycle. For this reason SR1, a mutant of GroEL that forms only single rings, cannot function as a chaperone. Mutations in SR1 that restore chaperone function weaken its interaction with the cochaperonin GroES. We predicted that GroES mutants with reduced affinity for GroEL would also restore function to SR1. To test this, we mutated residues in GroES in and near its contact site with GroEL. Nearly half of the mutants showed partial function with SR1. Two mutants were confirmed to have reduced affinity for GroEL. Intriguingly, some GroES mutants were able to function with active single ring mutants of GroEL.