10.1371/journal.pone.0078135.g009
Toshifumi Mizuta
Toshifumi
Mizuta
Kasumi Ando
Kasumi
Ando
Tatsuya Uemura
Tatsuya
Uemura
Yasushi Kawata
Yasushi
Kawata
Tomohiro Mizobata
Tomohiro
Mizobata
Proposed sequence of events for GroEL encapsulation, based upon results from the present study.
Public Library of Science
2013
Dynamic Process
chaperonin function
GroEL apical domain
GroEL D 398A variants
apical domain movement
GroEL rings
GroEL SR
ATP binding
circularly permuted GroEL
polypeptide ends
GroES binding
Escherichia coli GroEL Kinetic analyses
CP
GroEL mutants
Helix M
ATP binding site
2013-10-30 19:52:53
Dataset
https://plos.figshare.com/articles/dataset/_Proposed_sequence_of_events_for_GroEL_encapsulation_based_upon_results_from_the_present_study_/837360
<p>In this figure, ideas derived from the present study are illustrated in <i>yellow text bubbles</i>, ideas based upon prior studies <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0078135#pone.0078135-Yoshimi1" target="_blank">[20]</a>–<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0078135#pone.0078135-Mizobata1" target="_blank">[22]</a> are illustrated in the <i>blue text bubble</i>. The scheme is based on the characteristics displayed by numerous mutant forms of GroEL that highlight certain dependencies between individual molecular events. Kinetic phases detected in our stopped-flow experiments are indicated in <i>blue text</i>, names of individual mutants are denoted in <i>red text</i>, and <i>green text</i> indicates proposed correlations and conclusions derived from comparisons of our results with various previous studies. Details are given in the main text.</p>