#Chaperonin pdf
#Chaperonin series

Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins.

Kandror O, Sherman M, Rhode M, Goldberg AL.

Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding.

Jackson GS, Staniforth RA, Halsall DJ, Atkinson T, Holbrook JJ, Clarke AR, Burston SG.

Kinetics versus thermodynamics in protein folding. The formation of protein disulphide bonds. Calnexin: a membrane-bound chaperone of the endoplasmic reticulum.

Bergeron JJ, Brenner MB, Thomas DY, Williams DB.

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.

Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH.

Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent.

Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP.

Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor.

Chernoff YO, Lindquist SL, Ono B, Inge-Vechtomov SG, Liebman SW.

coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY. Six-fold rotational symmetry of ClpQ, the E.

Kessel M, Wu W, Gottesman S, Kocsis E, Steven AC, Maurizi MR.

Purification and characterization of ATP-induced structural changes. Structural analysis of substrate binding by the molecular chaperone DnaK.

Zhu X, Zhao X, Burkholder WF, Gragerov A, Ogata CM, Gottesman ME, Hendrickson WA.

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Flaherty KM, DeLuca-Flaherty C, McKay DB.Interaction of Hsp70 chaperones with substrates. A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. Lee GJ, Roseman AM, Saibil HR, Vierling E.Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. Ehrnsperger M, Gräber S, Gaestel M, Buchner J.Molecular chaperones in cellular protein folding. Principles that govern the folding of protein chains. This may not be the complete list of references from this article.

#Chaperonin pdf

The Full Text of this article is available as a PDF (587K). If the released substrate protein is still not correctly folded, it will go through another round of interaction with GroEL. Similarly, ATP binding, but not hydrolysis, in the opposite GroEL ring is needed to release GroES, thus opening the chamber. For proteins whose folding is absolutely dependent on the full GroE system, ATP binding (but not hydrolysis) in the encapsulating ring is needed to initiate protein folding. In the presence of ATP, GroES binds to GroEL, forming a large chamber that encapsulates substrate proteins for folding.

#Chaperonin series

ATP binding initiates a series of dramatic conformational changes that bury the substrate-binding sites, lowering the affinity for non-native polypeptide. The action of the ATPase cycle causes the substrate-binding surface of GroEL to alternate in character between hydrophobic (binding/unfolding) and hydrophilic (release/folding). Together with its co-protein GroES, GroEL binds non-native polypeptides and facilitates their refolding in an ATP-dependent manner. The chaperonins are large, double-ring oligomeric proteins that act as containers for the folding of other protein subunits. There has been great progress in understanding the structure and mechanism of action of the chaperonin family, exemplified by Escherichia coli GroEL. The molecular chaperones are a diverse set of protein families required for the correct folding, transport and degradation of other proteins in vivo.