PMID- 10196153 OWN - NLM STAT- MEDLINE DCOM- 19990517 LR - 20210209 IS - 0021-9258 (Print) IS - 0021-9258 (Linking) VI - 274 IP - 16 DP - 1999 Apr 16 TI - "Half of the sites" binding of D-glyceraldehyde-3-phosphate dehydrogenase folding intermediate with GroEL. PG - 10790-4 AB - Two D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) folding intermediate subunits bind with chaperonin 60 (GroEL) to form a stable complex, which can no longer bind with additional GAPDH intermediate subunits, but does bind with one more lysozyme folding intermediate or one chaperonin 10 (GroES) molecule, suggesting that the two GAPDH subunits bind at one end of the GroEL molecule displaying a "half of the sites" binding profile. For lysozyme, GroEL binds with either one or two folding intermediates to form a stable 1:1 or 1:2 complex with one substrate on each end of the GroEL double ring for the latter. The 1:1 complex of GroEL.GroES binds with one lysozyme or one dimeric GAPDH folding intermediate to form a stable ternary complex. Both complexes of GroEL.lysozyme1 and GroEL.GAPDH2 bind with one GroES molecule only at the other end of the GroEL molecule forming a trans ternary complex. According to the stoichiometry of GroEL binding with the GAPDH folding intermediate and the formation of ternary complexes containing GroEL.GAPDH2, it is suggested that the folding intermediate of GAPDH binds, very likely in the dimeric form, with GroEL at one end only. FAU - Li, J AU - Li J AD - National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing 100101, China. FAU - Wang, C C AU - Wang CC LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't PL - United States TA - J Biol Chem JT - The Journal of biological chemistry JID - 2985121R RN - 0 (Chaperonin 60) RN - EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases) RN - EC 3.2.1.17 (Muramidase) SB - IM MH - Binding Sites MH - Chaperonin 60/*metabolism MH - Enzyme Activation MH - Glyceraldehyde-3-Phosphate Dehydrogenases/chemistry/*metabolism MH - Muramidase/metabolism MH - Oxidation-Reduction MH - Protein Denaturation MH - Protein Folding EDAT- 1999/04/10 00:00 MHDA- 1999/04/10 00:01 CRDT- 1999/04/10 00:00 PHST- 1999/04/10 00:00 [pubmed] PHST- 1999/04/10 00:01 [medline] PHST- 1999/04/10 00:00 [entrez] AID - S0021-9258(19)73572-8 [pii] AID - 10.1074/jbc.274.16.10790 [doi] PST - ppublish SO - J Biol Chem. 1999 Apr 16;274(16):10790-4. doi: 10.1074/jbc.274.16.10790.