Sparrer, Helmut and Buchner, Johannes (1997) How GroES regulates binding of nonnative protein to GroEL. JOURNAL OF BIOLOGICAL CHEMISTRY, 272 (22). pp. 14080-14086. ISSN 0021-9258, 1083-351X
Full text not available from this repository.Abstract
At present, it is still enigmatic how the reaction cycle by which the Escherichia coli GroE chaperones mediate protein folding in the cell is coordinated with respect to the sequential order of binding and release of GroES, nucleotide, and nonnative protein. It is generally assumed that the asymmetric GroEL.GroES complex is the acceptor state for substrate protein, Nevertheless, this species is poorly understood in its binding characteristics for nucleotide and nonnative protein, We show here that this species has a high affinity binding site for nonnative protein. In addition to this, binding of nucleotide to one GroEL ring is strongly favored by GroES binding to the other ring, However, the slow rate of release of substrate protein from the unproductive trans-position kinetically favors the binding of a second GroES, thereby forming a symmetric GroEL(14).(GroES(7))(2) complex and simultaneously ensuring that substrate protein is sequestered in a position underneath GroES. Our results demonstrate that the intrinsic binding characteristics of the trans-bullet complex determine the sequence of events during the reaction cycle.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ESCHERICHIA-COLI; CHAPERONIN GROEL; CYCLE; COOPERATIVITY; MECHANISM; RELEASE; RECONSTITUTION; POLYPEPTIDES; AGGREGATION; HYDROLYSIS |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 27 Apr 2023 09:18 |
| Last Modified: | 27 Apr 2023 09:18 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50813 |
Actions (login required)
 |
View Item |
