caa a22 4500 47574408X CHVBK 20180406123508.0 cr unu---uuuuu 170329e20001001xx s 000 0 eng 10.1023/A:1007146217946 doi (NATIONALLICENCE)springer-10.1023/A:1007146217946 GroEL and Protein Disulfide Isomerase Each Binds with Folding Intermediates of D-Glyceraldehyde-3-Phosphate Dehydrogenase Released from Complexes Formed with the Other [Elektronische Daten] [Nian-xiang Zhang, Jian Li, Chih-chen Wang] Simultaneous presence of two chaperones, GroEL and protein disulfide isomerase (PDI), assists the reactivation of denatured D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in an additive way. Delayed addition of chaperones to the refolding solution after dilution of denatured GAPDH indicates an interaction with intermediates formed mainly in the first 5 min for PDI and formed within a longer time period for GroEL-ATP. The above indicate that the two chaperones interact with different folding intermediates of GAPDH. After delayed addition of one chaperone to the refolding mixture containing the other at 4°C, GroEL binds with all GAPDH intermediates dissociated from PDI, and PDI interacts with the intermediates released from GroEL during the first 10-20 min. It is suggested that the GAPDH folding intermediates released from the chaperone-bound complex are still partially folded so as to be rebound by the other chaperone. The above results clearly support the network model of GroEL and PDI. Plenum Publishing Corporation, 2000 Chaperone action nationallicence assisted folding nationallicence folding intermediate nationallicence GAPDH nationallicence GroEL nationallicence PDI nationallicence Zhang Nian-xiang Institute of Biophysics, Academia Sinica, National Laboratory of Biomacromolecules, 100101, Beijing, China aut Li Jian Institute of Biophysics, Academia Sinica, National Laboratory of Biomacromolecules, 100101, Beijing, China aut Wang Chih-chen Institute of Biophysics, Academia Sinica, National Laboratory of Biomacromolecules, 100101, Beijing, China aut Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/7(2000-10-01), 569-574 0277-8033 19:7<569 2000 19 10930 https://doi.org/10.1023/A:1007146217946 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1007146217946 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Zhang Nian-xiang Institute of Biophysics, Academia Sinica, National Laboratory of Biomacromolecules, 100101, Beijing, China aut NATIONALLICENCE 700 1- Li Jian Institute of Biophysics, Academia Sinica, National Laboratory of Biomacromolecules, 100101, Beijing, China aut NATIONALLICENCE 700 1- Wang Chih-chen Institute of Biophysics, Academia Sinica, National Laboratory of Biomacromolecules, 100101, Beijing, China aut NATIONALLICENCE 773 0- Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/7(2000-10-01), 569-574 0277-8033 19:7<569 2000 19 10930 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer