Author
Listed:
- Young Jun An
(Korea Institute of Ocean Science and Technology)
- Sara E. Rowland
(University of Maryland
Institute of Marine and Environmental Technology)
- Jung-Hyun Na
(Ewha Womans University)
- Dario Spigolon
(University of Maryland
Institute of Marine and Environmental Technology)
- 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
Institute of Marine and Environmental Technology)
- Sun-Shin Cha
(Ewha Womans University)
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.
Suggested Citation
Young Jun An & Sara E. Rowland & Jung-Hyun Na & Dario Spigolon & Seung Kon Hong & Yeo Joon Yoon & Jung-Hyun Lee & Frank T. Robb & Sun-Shin Cha, 2017.
"Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium,"
Nature Communications, Nature, vol. 8(1), pages 1-11, December.
Handle:
RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00980-z
DOI: 10.1038/s41467-017-00980-z
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