GroES dissociates from GroEL every:
| Range | 10 - 15 sec |
|---|---|
| Organism | Bacteria Escherichia coli |
| Reference | Kerner MJ, Naylor DJ, Ishihama Y, Maier T, Chang HC, Stines AP, Georgopoulos C, Frishman D, Hayer-Hartl M, Mann M, Hartl FU. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell. 2005 Jul 29 122(2):209-20. p.210 left column top paragraphPubMed ID16051146 |
| Primary Source | Fenton WA, Horwich AL. Chaperonin-mediated protein folding: fate of substrate polypeptide. Q Rev Biophys. 2003 May36(2):229-56. & Hartl FU, Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science. 2002 Mar 8 295(5561):1852-8.PubMed ID14686103, 11884745 |
| Comments | "GroES dissociates from GroEL every 10–15 s in a reaction dependent on the GroEL ATPase, thus allowing for the release of folded substrate and the recapture of incompletely folded protein (reviewed in primary sources)." |
| Entered by | Uri M |
| ID | 110574 |