Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES
Article Abstract:
The productive folding and release of polypeptides takes place in the central cavity of the GroEL protein which also contains the GroES protein. The protein folding activity of GroEL requires the presence of GroES and ATP. The polypeptide first binds to GroEL in the trans conformation. GroEL in this conformation contains no bound GroES. During protein folding, ATP hydrolysis causes the release of GroES while GroEL forms a cis complex. GroES then rebinds to the ring of GroEL containing the polypeptide. The polypeptide is sequestrated under the GroES in the complex.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
Deadly conformations: protein misfolding in prion disease
Article Abstract:
The transmission of prion diseases such bovine spongiform encepalopathy in cows or Creutzfeld-Jacob disease in humans was mediated by cannibalism and genetic inheritance. Genetic experiments dealing with the transmission mechanisms of prion diseases indicated the role of the cerebral PrP protein in promoting spongiform encepalopathies. The PrP protein was also characterized as a component of the disease process that undergoes changes in conformation to an insoluble and highly infective beta sheet state.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
User Contributions:
Comment about this article or add new information about this topic:
The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL
Article Abstract:
A map of substrate-binding domain movements of the GroEL chaperonin protein was constructed by utilizing cryo-electron microscopy and three-dimensional reconstruction. A large collection of hinge rotations and distortions was detected in the substrate- and GroEL-binding sites located in the apical domains of the chaperonin. Furthermore, the linkage between the rings exhibited allosteric switching by utilizing a direct connection to the adenosine triphosphate binding site.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Regulation of chromosomal replication in E. coli: sequestration and beyond. E. coli SeqA protein binds oriC in two different methyl-modulated reactions appropriate to its roles in DNA replication initiation and origin sequestration
- Abstracts: Antigenic variation in malaria. A developmentally regulated position effect at a telomeric locus in Trypanosoma brucei
- Abstracts: Components and dynamics of DNA replication complexes in S. cerevisiae: redistribution of MCM proteins and Cdc45p during S phase