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

FEBS Letters

Todd, Matthew J.¹  Lorimer, George H.¹  Boudkin, Olga²  Freire, Ernesto² 

[1] Dupont Co. Experimental Station, Central Research and Development Department, Wilmington, DE 19880-0402, USA;Biocalorimetry Center, Department of Biology, The Johns Hopkins University, Baltimore, MD 21218, USA

关键词: Protein folding;    Chaperone;    GroES;    Calorimetry;    Nucleotide binding;   

DOI  :  10.1016/0014-5793(95)00021-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown