Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins

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 surviv...

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Main Authors: Chaston, Jessica J., Smits, Callum, Aragão, David, Ahsan, Bilal, Sandin, Sara, Stock, Daniela, Wong, Andrew S. W., Molugu, Sudheer K., Molugu, Sanjay K., Bernal, Ricardo A., Stewart, Alastair G.
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2016
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Online Access:https://hdl.handle.net/10356/80266
http://hdl.handle.net/10220/40448
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-802662023-02-28T16:58:06Z Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins Chaston, Jessica J. Smits, Callum Aragão, David Ahsan, Bilal Sandin, Sara Stock, Daniela Wong, Andrew S. W. Molugu, Sudheer K. Molugu, Sanjay K. Bernal, Ricardo A. Stewart, Alastair G. School of Biological Sciences Biological Sciences 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. Accepted version 2016-04-15T06:39:10Z 2019-12-06T13:46:10Z 2016-04-15T06:39:10Z 2019-12-06T13:46:10Z 2016 Journal Article Chaston, J., Smits, C., Aragão, D., Wong, A., Ahsan, B., Sandin, S., et al. (2016). Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins. Structure, 24(3), 364-374. 0969-2126 https://hdl.handle.net/10356/80266 http://hdl.handle.net/10220/40448 10.1016/j.str.2015.12.016 en Structure © 2016 Elsevier. This is the author created version of a work that has been peer reviewed and accepted for publication by Structure, Elsevier. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://dx.doi.org/10.1016/j.str.2015.12.016]. 39 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Biological Sciences
spellingShingle Biological Sciences
Chaston, Jessica J.
Smits, Callum
Aragão, David
Ahsan, Bilal
Sandin, Sara
Stock, Daniela
Wong, Andrew S. W.
Molugu, Sudheer K.
Molugu, Sanjay K.
Bernal, Ricardo A.
Stewart, Alastair G.
Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins
description 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.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Chaston, Jessica J.
Smits, Callum
Aragão, David
Ahsan, Bilal
Sandin, Sara
Stock, Daniela
Wong, Andrew S. W.
Molugu, Sudheer K.
Molugu, Sanjay K.
Bernal, Ricardo A.
Stewart, Alastair G.
format Article
author Chaston, Jessica J.
Smits, Callum
Aragão, David
Ahsan, Bilal
Sandin, Sara
Stock, Daniela
Wong, Andrew S. W.
Molugu, Sudheer K.
Molugu, Sanjay K.
Bernal, Ricardo A.
Stewart, Alastair G.
author_sort Chaston, Jessica J.
title Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins
title_short Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins
title_full Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins
title_fullStr Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins
title_full_unstemmed Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins
title_sort structural and functional insights into the evolution and stress adaptation of type ii chaperonins
publishDate 2016
url https://hdl.handle.net/10356/80266
http://hdl.handle.net/10220/40448
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