Residues in chaperonin GroEL required for polypeptide binding and release

@article{Fenton1994ResiduesIC,
  title={Residues in chaperonin GroEL required for polypeptide binding and release},
  author={Wayne A. Fenton and Yechezkel Kashi and Krystyna Furtak and Arthur L. Norwich},
  journal={Nature},
  year={1994},
  volume={371},
  pages={614-619}
}
CHAPERONINS are ring-shaped protein complexes that are essential in the cell, mediating ATP-dependent polypeptide folding in a vari-ety of compartments1–3. Recent studies suggest that they function through multiple rounds of binding and release of non-native proteins: with each round of ATP-driven release into the bulk solution, a substrate protein kinetically partitions between folding to the native state or rebinding to another chaperonin molecule4–6. To gain further insight into the… Expand
Chaperonin complex with a newly folded protein encapsulated in the folding chamber
TLDR
Structures of gp23–chaperonin complexes are presented, showing both the initial captured state and the final, close-to-native state with gp23 encapsulated in the folding chamber, explaining why the GroEL–GroES complex is not able to fold gp23 and showing how the chaperon in structure distorts to enclose a large, physiological substrate protein. Expand
Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding.
TLDR
The GroEL-GroES-ADP7 crystal structure provided important insights into the GroEL ATPase mechanism, and the opening-out motion of GroEL subunits on binding GroES involves a downward rotation of the intermediate domain. Expand
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL.
  • R. Zahn, A. Buckle, +4 authors A. Fersht
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1996
The chaperonin GroEL is a large complex composed of 14 identical 57-kDa subunits that requires ATP and GroES for some of its activities. We find that a monomeric polypeptide corresponding to residuesExpand
Two families of chaperonin: physiology and mechanism.
TLDR
A number of issues under current study are discussed, including the range of substrates acted on by the two classes of chaperonin, in particular by GroEL in the bacterial cytoplasm and CCT in the eukaryotic cytosol, and are all these substrates subject to encapsulation. Expand
Mechanism of substrate recognition by the chaperonin GroEL.
  • W. Houry
  • Biology, Medicine
  • Biochemistry and cell biology = Biochimie et biologie cellulaire
  • 2001
TLDR
A model of substrate recognition by GroEL is proposed and it is proposed that binding takes place preferentially between the hydrophobic residues in the apical domains of GroEL and thehydrophobic faces exposed by the beta-sheets or alpha-helices in the alphabeta domains of protein substrates. Expand
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL.
TLDR
It is concluded that significant native-like structure is present in protein-folding intermediates bound to GroEL, and the pattern and magnitude of amide proton protection indicate that the central parallel beta-sheet found in native DHFR is presentIn a moderately stable state in GroEL-bound DHFR. Expand
Chaperonin-mediated folding of viral proteins.
TLDR
The phiEL chaper onin from phage EL is revealed to be the first virally encoded chaperonin and is proposed to function independently of the host chaperOnin machinery. Expand
Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding
TLDR
It is concluded that GroEL, in general, behaves passively with respect to its substrate proteins during these steps, and chamber-mediated folding appears to resemble folding in solution, except that major kinetic complications of multimolecular association are prevented. Expand
Chaperonin-mediated protein folding: fate of substrate polypeptide
TLDR
Questions about the folding of substrates too large to be encapsulated inside the machine and means of further resolving the states of chaperonin-associated polypeptide are discussed are discussed. Expand
The substrate recognition mechanisms in chaperonins
TLDR
Chaperonins are large oligomers assembled into ring structures that enclose a cavity in which folding takes place, and for this process to occur, the chaperonin must first recognize and interact with the unfolded polypeptide, then undergo a conformational change upon nucleotide binding that results in the closure of the cavity which in turn mediates the folding reaction inside the cavity. Expand
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References

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GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
TLDR
It is found that, upon addition of ATP and the cochaperonin GroES, polypeptide is released rapidly from GroEL in a predominantly nonnative conformation that can be trapped by mutant forms of GroEL that are capable of binding but not releasing substrate. Expand
Location of a folding protein and shape changes in GroEL–GroES complexes imaged by cryo-electron microscopy
TLDR
The first direct visualization, by cryo-electron microscopy, of a non-native protein substrate (malate dehydrogenase) bound to the mobile, outer domains at one end of GroEL is reported. Expand
Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding.
TLDR
A unifying model for chaperonin-facilitated protein folding based on successive rounds of binding and release, and partitioning between committed and kinetically trapped intermediates, is proposed. Expand
Characterization of a functionally important mobile domain of GroES
TLDR
It is reported that native GroES has a highly mobile and accessible polypeptide loop whose mobility and accessibility are lost upon formation of the GroES/GroEL complex. Expand
Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
TLDR
It is concluded that GroEL indeed is a machine at the distal end of the pathway of transfer of genetic information, assisting a large and specific set of newly translated cytoplasmic proteins to reach their native tertiary structures. Expand
A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin
TLDR
It is shown that in the presence of Mg-ATP alone, alpha- and beta-tubulin target proteins are discharged from cytoplasmic chaperonin in a nonnative form and cofactors participate in the folding process and do not merely trigger release. Expand
Symmetric complexes of GroE chaperonins as part of the functional cycle.
TLDR
The existence of symmetric chaperonin complexes is not predicted by current models of the functional cycle for GroE-mediated protein folding, but they are proposed to be functionally significant. Expand
Chaperonin‐mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity.
TLDR
The functional complex of GroEL and GroES is characterized by asymmetrical binding of GroES to one end of the GroEL cylinder and it is suggested that binding of the substrate protein occurs within the central cavity ofGroEL. Expand
Different conformations for the same polypeptide bound to chaperones DnaK and GroEL
TLDR
Transferred nuclear Overhauser effects are analysed in two-dimensional NMR spectra and show that the peptide is in an extended conformation while bound to DnaK but is helical when bound to GroEL, whereas the side chains are less mobile when boundto GroEL. Expand
A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
TLDR
It is suggested that TF55 in archaebacteria and TCP1 in the eukaryotic cytosol are members of a new class of molecular chaperones. Expand
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