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Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein.
Cell. 2006 Jun 02; 125(5):903-14.Cell

Abstract

GroEL and GroES form a chaperonin nano-cage for proteins up to approximately 60 kDa to fold in isolation. Here we explored the structural features of the chaperonin cage critical for rapid folding of encapsulated substrates. Modulating the volume of the GroEL central cavity affected folding speed in accordance with confinement theory. Small proteins (approximately 30 kDa) folded more rapidly as the size of the cage was gradually reduced to a point where restriction in space slowed folding dramatically. For larger proteins (approximately 40-50 kDa), either expanding or reducing cage volume decelerated folding. Additionally, interactions with the C-terminal, mildly hydrophobic Gly-Gly-Met repeat sequences of GroEL protruding into the cavity, and repulsion effects from the negatively charged cavity wall were required for rapid folding of some proteins. We suggest that by combining these features, the chaperonin cage provides a physical environment optimized to catalyze the structural annealing of proteins with kinetically complex folding pathways.

Authors+Show Affiliations

Tang YC
Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
Chang HC
No affiliation info available
Roeben A
No affiliation info available
Wischnewski D
No affiliation info available
Wischnewski N
No affiliation info available
Kerner MJ
No affiliation info available
Hartl FU
No affiliation info available
Hayer-Hartl M
No affiliation info available

MeSH

Amino Acid SequenceBacterial ProteinsChaperonin 10Chaperonin 60Escherichia coliModels, MolecularMolecular WeightMutationProtein ConformationProtein FoldingProtein Structure, Tertiary

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16751100

Citation

Tang, Yun-Chi, et al. "Structural Features of the GroEL-GroES Nano-cage Required for Rapid Folding of Encapsulated Protein." Cell, vol. 125, no. 5, 2006, pp. 903-14.
Tang YC, Chang HC, Roeben A, et al. Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell. 2006;125(5):903-14.
Tang, Y. C., Chang, H. C., Roeben, A., Wischnewski, D., Wischnewski, N., Kerner, M. J., Hartl, F. U., & Hayer-Hartl, M. (2006). Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell, 125(5), 903-14.
Tang YC, et al. Structural Features of the GroEL-GroES Nano-cage Required for Rapid Folding of Encapsulated Protein. Cell. 2006 Jun 2;125(5):903-14. PubMed PMID: 16751100.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. AU - Tang,Yun-Chi, AU - Chang,Hung-Chun, AU - Roeben,Annette, AU - Wischnewski,Dirk, AU - Wischnewski,Nadine, AU - Kerner,Michael J, AU - Hartl,F Ulrich, AU - Hayer-Hartl,Manajit, PY - 2006/02/15/received PY - 2006/03/29/revised PY - 2006/04/04/accepted PY - 2006/6/6/pubmed PY - 2006/7/27/medline PY - 2006/6/6/entrez SP - 903 EP - 14 JF - Cell JO - Cell VL - 125 IS - 5 N2 - GroEL and GroES form a chaperonin nano-cage for proteins up to approximately 60 kDa to fold in isolation. Here we explored the structural features of the chaperonin cage critical for rapid folding of encapsulated substrates. Modulating the volume of the GroEL central cavity affected folding speed in accordance with confinement theory. Small proteins (approximately 30 kDa) folded more rapidly as the size of the cage was gradually reduced to a point where restriction in space slowed folding dramatically. For larger proteins (approximately 40-50 kDa), either expanding or reducing cage volume decelerated folding. Additionally, interactions with the C-terminal, mildly hydrophobic Gly-Gly-Met repeat sequences of GroEL protruding into the cavity, and repulsion effects from the negatively charged cavity wall were required for rapid folding of some proteins. We suggest that by combining these features, the chaperonin cage provides a physical environment optimized to catalyze the structural annealing of proteins with kinetically complex folding pathways. SN - 0092-8674 UR - https://www.unboundmedicine.com/medline/citation/16751100/Structural_features_of_the_GroEL_GroES_nano_cage_required_for_rapid_folding_of_encapsulated_protein_ DB - PRIME DP - Unbound Medicine ER -