Range: 250 different proteins
||Bacteria Escherichia coli
||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.213 left column bottom paragraph, p.214 left column bottom paragraph & p.217 left column bottom paragraphPubMed ID16051146
||Ewalt KL, Hendrick JP, Houry WA, Hartl FU. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell. 1997 Aug 8 90(3):491-500. & Houry WA, Frishman D, Eckerskorn C, Lottspeich F, Hartl FU. Identification of in vivo substrates of the chaperonin GroEL. Nature. 1999 Nov 11 402(6758):147-54.PubMed ID9267029, 10647006
||"A total of ~250 proteins were reproducibly identified as specifically associated with GroEL at 30°C and 37°C ...Based on quantitative proteomic analysis by SILAC (stable isotope labeling by amino acids in cell culture) (Ong et al., 2002), [researchers] deduced criteria to assign the ~250 GroEL interactors to the three substrate classes found in the initial set of test proteins...About 250 different proteins interact with GroEL under normal growth conditions of E. coli, consistent with previous estimates (primary sources)."