GroES

GroEL and GroES are E.coli chaperonins, which are homologs of mitochondrial chaperonins Hsp60 and Hsp10. GroEL is a double toriodal assembly of 14 identical subunits which form two heptameric rings stacked back-to-back, with a cavity at each end. GroEL and its co-chaperonin GroES facilitate protein folding with an ATP-dependent mechanism. A proposed nested model for cooperatively in ATP binding by GroEL suggests that each ring of GroEL is in equilibrium between a tense protein-acceptor (T) state and a relaxed protein-release (R) state. The T state has low affinity for ATP and high affinity for unfolded polypeptide substrates whereas the R state has a high affinity for ATP and low affinity for unfolded polypeptides substrates (2). Recent electron cryomicroscopy data demonstrates that the GroEL double-ring particle is in equilibrium between three allosteric states TT, TR and RR (3). Non-native conformations of diverse protein substrates bind to the apical domains surrounding the opening of the double toroid

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SPECIFICATIONS

Catalog Number

G8980-25

Size

50ul

Applications

IP, WB

Hosts

Rabbit

Form

Serum

P Type

Pab

Purity

Serum

Isotype

IgG

References

1. Chandrasekhar, G.N., Tilly, K., Woolford, C., Hendrix, R. and Georgopoulos, C. (1986) \nJ. Biol. Chem. 261: 12414-12419. \n2. Yifrach, O. and Horovitz, A. (1996) J. Mol. Biol. 255: 356-361. \n3. White, H.E., Chen, S., Roseman, A.M., Yifrach, O., Horovitz, A. and Saibil, H.R. (1997) \nNat. Struct. Biol. 4: 690-694. \n4. Yifrach, O. and Horovitz, A. (2000) PNAS USA 97: 1521-1524. \n5. Kandror, O., Sherman, M. and Goldberg, A. (1999) J. Biol. Chem. 274: 37743-37749. \n6. Bang, H., et al. (2000) Eur. J. Biochem. 267: 3270-3280. \n7. Yeh, C.H., Chang, P.F.L., Yeh, K.W., Lin, W.C., Chen, Y.M., Lin, C.Y. (1997) Proc \nNatl Acad Sci USA 94(20): 10967-10972. \n

Additional Info

Detects a ~10kD protein, corresponding to the apparent molecular mass of GroES on SDS-PAGE immunoblots, in samples from E. coli. This antibody has not been tested for crossreactivity to other bacterial species.