GroES and the chaperonin-assisted protein folding cycle: GroES has no affinity for nucleotides

Matthew J. Todd, Olga Boudkin, Ernesto Freire, George H. Lorimer

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)123-125
Number of pages3
JournalFEBS Letters
Volume359
Issue number2-3
DOIs
StatePublished - Feb 13 1995

Keywords

  • Calorimetry
  • Chaperone
  • GroES
  • Nucleotide binding
  • Protein folding

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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