Structural Features of the GroEL-GroES Nano-Cage Required for Rapid Folding of Encapsulated Protein Export

@article{citeulike:1299828, abstract = {Summary GroEL and GroES form a chaperonin nano-cage for proteins up to \~{}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 (\~{}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 (\~{}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.}, author = {Tang, Yun-Chi and Chang, Hung-Chun and Roeben, Annette and Wischnewski, Dirk and Wischnewski, Nadine and Kerner, Michael J. and Hartl, Ulrich F. and Hayer-Hartl, Manajit}, citeulike-article-id = {1299828}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.cell.2006.04.027}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0092867406005605}, citeulike-linkout-2 = {http://www.sciencedirect.com/science/article/B6WSN-4K47W5D-H/2/98731806fa157491d3ab15fb53ae7ead}, day = {2}, doi = {10.1016/j.cell.2006.04.027}, journal = {Cell}, keywords = {folding, groel, groel-substrate}, month = {June}, number = {5}, pages = {903--914}, posted-at = {2009-06-03 21:42:11}, priority = {2}, title = {Structural Features of the GroEL-GroES Nano-Cage Required for Rapid Folding of Encapsulated Protein}, url = {http://dx.doi.org/10.1016/j.cell.2006.04.027}, volume = {125}, year = {2006} }

TY - JOUR ID - citeulike:1299828 L3 - citeulike-article-id:1299828 N2 - Summary GroEL and GroES form a chaperonin nano-cage for proteins up to ~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 (~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 (~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. IS - 5 JF - Cell EP - 914 TI - Structural Features of the GroEL-GroES Nano-Cage Required for Rapid Folding of Encapsulated Protein VL - 125 SP - 903 KW - folding KW - groel KW - groel-substrate AU - Tang, Yun-Chi AU - Chang, Hung-Chun AU - Roeben, Annette AU - Wischnewski, Dirk AU - Wischnewski, Nadine AU - Kerner, Michael AU - Hartl, Ulrich AU - Hayer-Hartl, Manajit PY - 2006/06/02/ UR - http://dx.doi.org/10.1016/j.cell.2006.04.027 ER -