Nucleotide specificity of an archaeal group II chaperonin from Thermococcus strain KS‐1 with reference to the ATP‐dependent protein folding cycle

FEBS Letters

Yoshida, Takao¹  Maruyama, Tadashi¹  Kawaguchi, Rika² 

[1] Marine Biotechnology Institute Co. Ltd., Kamaishi Laboratories, 3-75-1 Heita Kamaishi, Iwate 026-0001, Japan;School of Fisheries Sciences, Kitasato University, Okkirai, Sanriku, Iwate 022-0101, Japan

关键词: Archaea;    ATPase cycle;    Group II chaperonin;    Molecular chaperone;    Nucleoside specificity;    Protein folding;    α16mer;    α-subunit homo-oligomer;    β16mer;    β-subunit homo-oligomer;    GFP;    green fluorescent protein;    HPLC;    high-performance liquid chromatography;    nαβ16mer;    natural chaperonin oligomer;   

DOI  :  10.1016/S0014-5793(02)02377-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The archaeal chaperonin-mediated folding of green fluorescent protein (GFP) was examined in the presence of various nucleotides. The recombinant α- and β-subunit homo-oligomers and natural chaperonin oligomer from Thermococcus strain KS-1 exhibited folding activity with not only ATP but also with CTP, GTP, or UTP. The ADP-bound form of both recombinant and natural chaperonin had the ability to capture non-native GFP, but could not refold it in the presence of CTP, GTP or UTP until ATP was supplied. The archaeal chaperonin thus utilized ATP, but could not use other nucleoside triphosphates in the cytoplasm where ADP was present.

【 授权许可】

Unknown