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10 results on '"Spigolon, Dario"'

2. Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog

Author

Spigolon, Dario, primary, Gallagher, D. Travis, additional, Velazquez-Campoy, Adrian, additional, Bulone, Donatella, additional, Narang, Jatin, additional, San Biagio, Pier Luigi, additional, Cappello, Francesco, additional, Macario, Alberto J.L., additional, Conway de Macario, Everly, additional, and Robb, Frank T., additional

Published
2017
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5. Hsp60, amateur chaperone in amyloid-beta fibrillogenesis

Author

Mangione, Maria Rosalia, primary, Vilasi, Silvia, additional, Marino, Claudia, additional, Librizzi, Fabio, additional, Canale, Claudio, additional, Spigolon, Dario, additional, Bucchieri, Fabio, additional, Fucarino, Alberto, additional, Passantino, Rosa, additional, Cappello, Francesco, additional, Bulone, Donatella, additional, and San Biagio, Pier Luigi, additional

Published
2016
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7. Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacterium.

Author

Young Jun An, Rowland, Sara E., Jung-Hyun Na, Spigolon, Dario, Seung Kon Hong, Yeo Joon Yoon, Jung-Hyun Lee, Robb, Frank T., and Sun-Shin Cha

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. [ABSTRACT FROM AUTHOR]

Published
2017
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10. Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog

Author

Alberto J.L. Macario, Adrián Velázquez-Campoy, Jatin Narang, Dario Spigolon, Frank T. Robb, Everly Conway de Macario, Donatella Bulone, Francesco Cappello, D. Travis Gallagher, Pier Luigi San Biagio, Spigolon, Dario, Gallagher, D. Travi, Velazquez-Campoy, Adrian, Bulone, Donatella, Narang, Jatin, San Biagio, Pier Luigi, Cappello, Francesco, Macario, Alberto J.L., Conway de Macario, Everly, and Robb, Frank T.

Subjects
0301 basic medicine, Protein subunit, Mutant, Biophysics, Heterologous, Biochemistry, Chaperonin, lcsh:Biochemistry, 03 medical and health sciences, DSC, differential scanning calorimetry, CCT% chaperonin, Pf, Pyrococcus furiosus, Denaturation (biochemistry), lcsh:QD415-436, Molecular Biology, lcsh:QH301-705.5, DLS, dynamic light scattering, biology, ITC, isothermal titration calorimetry, Wild type, Isothermal titration calorimetry, Cell Biology, Chaperonopathies, biology.organism_classification, Protein calorimetry, Neuropathy, Pyrococcus furiosus, 030104 developmental biology, Biophysic, lcsh:Biology (General), Chaperonopathie, CCT5, Pyrococcus furiosu, Research Article, Pf-CD1, Pyrococcus furiosus chaperonin subunit with the last 22 amino acids deleted
Abstract

The human chaperonin complex is a ~ 1 MDa nanomachine composed of two octameric rings formed from eight similar but non-identical subunits called CCT. Here, we are elucidating the mechanism of a heritable CCT5 subunit mutation that causes profound neuropathy in humans. In previous work, we introduced an equivalent mutation in an archaeal chaperonin that assembles into two octameric rings like in humans but in which all subunits are identical. We reported that the hexadecamer formed by the mutant subunit is unstable with impaired chaperoning functions. This study quantifies the loss of structural stability in the hexadecamer due to the pathogenic mutation, using differential scanning calorimetry (DSC) and isothermal titration calorimetry (ITC). The disassembly of the wild type complex, which is tightly coupled with subunit denaturation, was decoupled by the mutation without affecting the stability of individual subunits. Our results verify the effectiveness of the homo-hexadecameric archaeal chaperonin as a proxy to assess the impact of subtle defects in heterologous systems with mutations in a single subunit., Graphical abstract fx1, Highlights • A crippling hereditary neuropathy was addressed at the molecular level. • The archaeal/CCT5 model represents a promising testbed for subtle defects. • The homomeric archaeal model amplifies the effect of the mutation. • The mutation decouples assembly without destabilizing individual subunits.

Published
2017

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