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|Title:||Structural and Functional Insights into the Evolution and Stress Adaptation of Type II Chaperonins||Authors:||Chaston, Jessica J.
Wong, Andrew S. W.
Molugu, Sudheer K.
Molugu, Sanjay K.
Bernal, Ricardo A.
Stewart, Alastair G.
|Keywords:||Biological Sciences||Issue Date:||2016||Source:||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.||Series/Report no.:||Structure||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.||URI:||https://hdl.handle.net/10356/80266
|ISSN:||0969-2126||DOI:||http://dx.doi.org/10.1016/j.str.2015.12.016||Rights:||© 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].||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SBS Journal Articles|
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