Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium

Young Jun An, Sara E. Rowland, Jung-Hyun Na, Dario Spigolon, Seung Kon Hong, Yeo Joon Yoon, Jung-Hyun Lee, Frank T. Robb () and Sun-Shin Cha ()
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Young Jun An: Korea Institute of Ocean Science and Technology
Sara E. Rowland: University of Maryland
Jung-Hyun Na: Ewha Womans University
Dario Spigolon: University of Maryland
Seung Kon Hong: Ewha Womans University
Yeo Joon Yoon: Ewha Womans University
Jung-Hyun Lee: Korea Institute of Ocean Science and Technology
Frank T. Robb: University of Maryland
Sun-Shin Cha: Ewha Womans University

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: Abstract The chaperonins (CPNs) are megadalton sized hollow complexes with two cavities that open and close to encapsulate non-native proteins. CPNs are assigned to two sequence-related groups that have distinct allosteric mechanisms. In Group I CPNs a detachable co-chaperone, GroES, closes the chambers whereas in Group II a built-in lid closes the chambers. Group I CPNs have a bacterial ancestry, whereas Group II CPNs are archaeal in origin. Here we describe open and closed crystal structures representing a new phylogenetic branch of CPNs. These Group III CPNs are divergent in sequence and structure from extant CPNs, but are closed by a built-in lid like Group II CPNs. A nucleotide-sensing loop, present in both Group I and Group II CPNs, is notably absent. We identified inter-ring pivot joints that articulate during ring closure. These Group III CPNs likely represent a relic from the ancestral CPN that formed distinct bacterial and archaeal branches.

Date: 2017
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DOI: 10.1038/s41467-017-00980-z

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