Chaperonin GroE and ADP facilitate the folding of various proteins and protect against heat inactivation

FEBS Letters

Mizobata, Tomohiro¹  Nosaka, Koji¹  Hongo, Kunihiro¹  Kawata, Yasushi¹  Nagai, Jun¹ 

[1] Department of Biotechnology, Faculty of Engineering, Tottori University, Tottori 680, Japan

关键词: Chaperonin;    GroE;    Molecular chaperone;    Protein folding;    Protein heat stability;    GLUCDH;    glucose dehydrogenase;    Gdn-HCl;    guanidine hydrochloride;    LDH;    lactate dehydrogenase;    MDH;    malate dehydrogenase;    TAA;    Taka-amylase A;   

DOI  :  10.1016/0014-5793(94)00456-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In the presence of ADP, the molecular chaperones GroEL and GroES from Escherichia coli not only facilitated the refolding of various proteins, but also prevented their irreversible heat inactivation in vitro. Without nucleotides the refolding reactions were arrested by GroEL. Addition of GroES and ADP to the reaction mixture initiated at the refolding reactions and the enzyme activities were regained efficiently. The presence of GroE(GroEL and GroES) and ADP also protected against heat inactivation of native enzymes at various temperatures. These findings suggest that in the presence of GroES, nucleotide binding is an important event in the mechanism of GroEL-facilitated protein folding.

【 授权许可】

Unknown