Insights into structural details and energy usage of the group II chaperonin TRiC

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Abstract/Contents

Abstract
Chaperonins are a subset of molecular chaperones which assist in the protein folding process. These oligomeric chaperone complexes can be classified into two structurally distinct classes: group I, which are found in prokaryotes and endosymbiotic organelles, or group II, which are present in archaea and eukaryotes. The TCP-1 ring complex (TRiC) or CCT, is an essential, barrel-shaped group II chaperonin complex involved in folding approximately 10% of all proteins within the eukaryotic cytosol. While the general architecture of TRiC is understood, the exact arrangement of the 8 unique TRiC subunits (CCT1-8) within each ring, as well as the stacking between the two rings, has been debated for over a decade. This thesis includes data to support a specific arrangement for the TRiC complex based on results from mass spectrometry from crosslinked yeast and bovine TRiC, yeast ex vivo crosslinking, and probabilistic models. In addition, this work also characterizes the different affinities for ATP among CCT1-8 as well as their functional relevance in vivo. These developments contribute to the understanding of fundamental mechanisms regarding how TRiC mediates the folding of different protein substrates in the chaperonin-assisted folding process.

Description

Type of resource text
Form electronic; electronic resource; remote
Extent 1 online resource.
Publication date 2011
Issuance monographic
Language English

Creators/Contributors

Associated with Chen, Bryan Yu-Ann
Associated with Stanford University, Department of Biology.
Primary advisor Frydman, Judith
Thesis advisor Frydman, Judith
Thesis advisor Gozani, Or Pinchas
Thesis advisor Nelson, W. J. (W. James)
Thesis advisor Yang, Yanmin, Ph. D
Advisor Gozani, Or Pinchas
Advisor Nelson, W. J. (W. James)
Advisor Yang, Yanmin, Ph. D

Subjects

Genre Theses

Bibliographic information

Statement of responsibility Bryan Yu-Ann Chen.
Note Submitted to the Department of Biology.
Thesis Ph.D. Stanford University 2011
Location electronic resource

Access conditions

Copyright
© 2011 by Bryan Yu-Ann Chen
License
This work is licensed under a Creative Commons Attribution Non Commercial 3.0 Unported license (CC BY-NC).

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