Nucleotide specificity of an archaeal group II chaperonin from Thermococcus strain KS-1 with reference to the ATP-dependent protein folding cycle.
The archaeal chaperonin-mediated folding of green fluorescent protein (GFP) was examined in the presence of various nucleotides. The recombinant alpha- and beta-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.
Yoshida
Takao
T
Marine Biotechnology Institute Co. Ltd., Kamaishi Laboratories, 3-75-1 Heita Kamaishi, Iwate 026-0001, Japan.
Kawaguchi
Rika
R
Maruyama
Tadashi
T
D000244:Adenosine Diphosphate / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000737:chemistry*; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D018833:Chaperonins / Q000737:chemistry* / Q000378:metabolism*; D003570:Cytidine Triphosphate / Q000737:chemistry; D049452:Green Fluorescent Proteins; D006160:Guanosine Triphosphate / Q000737:chemistry; D006868:Hydrolysis; D008164:Luminescent Proteins / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D017510:Protein Folding; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D019712:Thermococcus / Q000737:chemistry*; D014544:Uridine Triphosphate / Q000737:chemistry
D019843:Archaeal Proteins; D008164:Luminescent Proteins; D021122:Protein Subunits; D011994:Recombinant Proteins; D049452:Green Fluorescent Proteins; D000244:Adenosine Diphosphate; D003570:Cytidine Triphosphate; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D018833:Chaperonins; D014544:Uridine Triphosphate