The conformational cycle of the chaperonin termini
Abstract/Contents
- Abstract
- Chaperonins are an essential family of molecular chaperones present in all three domains of life. They are large oligomeric complexes comprising two rings of 7-9 subunits related by twofold symmetry. Chaperonins engage unfolded or misfolded client proteins and encapsulate them in an isolated folding chamber in an ATP-dependent manner. The chaperonins are subdivided into two phyla, known simply as group I and group II. The group I chaperonins are found in bacteria and the endosymbiotic organelles mitochondria and chloroplasts, whereas group II chaperonins are principally encoded by archaeal and eukaryotic genomes. Less frequently, group II chaperonins may be found in bacterial genomes. The two groups of chaperonin share the same domain architecture, differing primarily in complex stoichiometry, inter-ring register, and the requirement of cofactors for client folding. This thesis concerns the structural dynamics of the terminal regions of both the group I and group II chaperonins. In particular, this work presents evidence from molecular dynamics simulations that the C-termini of the group I chaperonin undergo an ATP dependent conformational cycle with implications for substrate binding. Using a combination of crystallography and solution state nuclear magnetic resonance spectroscopy, the final chapter of the thesis establishes that the C-terminal conformational cycle hypothesized for the group I chaperonin is observed in a model group II chaperonin. Furthermore, that chapter introduces a heretofore unobserved N-terminal conformation of the group II chaperonin and demonstrates that both the N and C-termini influence the nucleotide usage of the enzyme.
Description
| Type of resource | text |
|---|---|
| Form | electronic; electronic resource; remote |
| Extent | 1 online resource. |
| Publication date | 2016 |
| Issuance | monographic |
| Language | English |
Creators/Contributors
| Associated with | Dalton, Kevin Michael |
|---|---|
| Associated with | Stanford University, Biophysics Program. |
| Primary advisor | Frydman, Judith |
| Primary advisor | Pande, Vijay |
| Thesis advisor | Frydman, Judith |
| Thesis advisor | Pande, Vijay |
| Thesis advisor | Bryant, Zev David |
| Thesis advisor | Puglisi, Joseph D |
| Advisor | Bryant, Zev David |
| Advisor | Puglisi, Joseph D |
Subjects
| Genre | Theses |
|---|
Bibliographic information
| Statement of responsibility | Kevin Michael Dalton. |
|---|---|
| Note | Submitted to the Program in Biophysics. |
| Thesis | Thesis (Ph.D.)--Stanford University, 2016. |
| Location | electronic resource |
Access conditions
- Copyright
- © 2016 by Kevin Michael Dalton
- License
- This work is licensed under a Creative Commons Attribution Non Commercial 3.0 Unported license (CC BY-NC).
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