Chaston, Jessica J and Smits, Callum and Aragão, David and Wong, Andrew S W and Ahsan, Bilal and Sandin, Sara and Molugu, Sudheer K and Molugu, Sanjay K and Bernal, Ricardo A and Stock, Daniela and Stewart, Alastair G (2016) Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins. Structure, 24 (3). pp.364-74. ISSN 1878-4186 (OA)
Full text not available from this repository.Abstract
Chaperonins are essential biological complexes assisting protein folding in all kingdoms of life. Whereas homooligomeric bacterial GroEL binds hydrophobic substrates non-specifically, the heterooligomeric eukaryotic CCT binds specifically to distinct classes of substrates. Sulfolobales, which survive in a wide range of temperatures, have evolved three different chaperonin subunits (α, β, γ) that form three distinct complexes tailored for different substrate classes at cold, normal, and elevated temperatures. The larger octadecameric β complexes cater for substrates under heat stress, whereas smaller hexadecameric αβ complexes prevail under normal conditions. The cold-shock complex contains all three subunits, consistent with greater substrate specificity. Structural analysis using crystallography and electron microscopy reveals the geometry of these complexes and shows a novel arrangement of the α and β subunits in the hexadecamer enabling incorporation of the γ subunit.
| Item Type: | Article |
|---|---|
| Additional Information: | This article is available for free from the publisher’s website (please click link above). |
| Subjects: | R Medicine > R Medicine (General) |
| Depositing User: | Repository Administrator |
| Date Deposited: | 14 Mar 2016 00:07 |
| Last Modified: | 15 Jan 2018 02:52 |
| URI: | https://eprints.victorchang.edu.au/id/eprint/390 |
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