Abstract
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.
Original language | English (US) |
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Pages (from-to) | 123-125 |
Number of pages | 3 |
Journal | FEBS Letters |
Volume | 359 |
Issue number | 2-3 |
DOIs | |
State | Published - Feb 13 1995 |
Keywords
- Calorimetry
- Chaperone
- GroES
- Nucleotide binding
- Protein folding
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology