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GroES and the chaperonin‐assisted protein folding cycle: GroES has no affinity for nucleotides
Author(s) -
Todd Matthew J.,
Boudkin Olga,
Freire Ernesto,
Lorimer George H.
Publication year - 1995
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(95)00021-z
Subject(s) - groes , groel , chaperonin , nucleotide , protein folding , folding (dsp implementation) , chaperone (clinical) , foldase , biology , chemistry , biochemistry , biophysics , escherichia coli , medicine , pathology , electrical engineering , gene , engineering
The E. coli chaperonin proteins, GroEL and GroES, assist in folding newly synthesized proteins. GroES is necessary for GroEL‐assisted folding under conditions where the substrate protein cannot spontaneously fold. On the basis of photolabelling of GroES with 8‐azido‐ATP, a role for nucleotide binding to GroES in chaperonin function was suggested [Martin, et al., Nature , 366 (1993) 279–2821]. We confirm the photolabelling of GroES with 8‐azido‐ATP. However, other proteins not known to contain nucleotide binding sites also become photolabeled suggesting that labeling is non‐specific. Using rigorous physical methods, isothermal calorimetry and equilibrium binding, no interaction between GroES and nucleotides could be detected. We conclude that GroES has no nucleotide binding site.