Multivalent binding of nonnative substrate proteins by the chaperonin GroEL

Cell

Volumn 100, Issue 5, 2000, Pages 561-573

  Farr, George W ^a   Furtak, Krystyna ^a   Rowland, Matthew B ^a   Ranson, Neil A ^b   Saibil, Helen R ^b   Kirchhausen, Tomas ^c   Horwich, Arthur L ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b UNIVERSITY OF LONDON   (United Kingdom)

^c HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN; MALATE DEHYDROGENASE; RIBULOSEBISPHOSPHATE CARBOXYLASE;

ARTICLE; BINDING SITE; ENZYME SUBSTRATE COMPLEX; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN FOLDING; RESIDUE ANALYSIS;

EID: 0034598920     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80692-3     Document Type: Article

References (28)

1. The crystal structure of the bacterial chaperonin GroEL at 2.8 Å
2. A carboxy-terminal deletion impairs the assembly of GroEL and confers a pleiotropic phenotype in Escherichia coli K12
3. Thermal motions of surface α-helices in the D-galactose chemosensory receptor
4. GroEL-mediated protein folding
5. Residues in chaperonin GroEL required for polypeptide binding and release
6. SPIDER and WEB: Processing and visualization of images in 3D electon microscopy and related fields
7. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and MgATP
8. Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding
9. Structural aspects of GroEL function
10. Folding in vivo of bacterial cytoplasmic proteins - Role of GroEL
11. Improved methods for building models in electron density maps and the location of errors in these models
12. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accomodates the protein substrate within its central cavity
13. Chaperonins can catalyze the reversal of early aggregation steps when a protein misfolds
14. Binding, encapsulation and ejection: Substrate dynamics during a chaperonin-assisted folding reaction
15. The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
16. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
17. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
18. On the role of groES in the chaperonin-assisted folding reaction
19. Chaperonin function: Folding by forced unfolding
20. Structure and function in GroEL-mediated protein folding
21. How GroES regulates binding of nonnative protein to GroEL
22. Chaperonin-facilitated protein folding: Optimization of rate and yield by an interative annealing mechanism
23. A thermodynamic coupling mechanism for GroEL-mediated unfolding
24. Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
25. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
26. 7 chaperonin complex
27. Catalysis of amide proteon exchange by the molecular chaperones GroEL and SecB