TY - JOUR
T1 - Stability and disassembly properties of human naïve Hsp60 and bacterial GroEL chaperonins
AU - Ricci, Caterina
AU - Ortore, Maria Grazia
AU - Vilasi, Silvia
AU - Carrotta, Rita
AU - Mangione, Maria Rosalia
AU - Bulone, Donatella
AU - Librizzi, Fabio
AU - Spinozzi, Francesco
AU - Burgio, Giosalba
AU - Amenitsch, Heinz
AU - San Biagio, Pier Luigi
PY - 2016/1/1
Y1 - 2016/1/1
N2 - Human Hsp60 chaperonin and its bacterial homolog GroEL, in association with the corresponding co-chaperonins Hsp10 and GroES, constitute important chaperone systems promoting the proper folding of several mitochondrial proteins. Hsp60 is also currently described as a ubiquitous molecule with multiple roles both in health conditions and in several diseases. Naïve Hsp60 bearing the mitochondrial import signal has been recently demonstrated to present different oligomeric organizations with respect to GroEL, suggesting new possible physiological functions. Here we present a combined investigation with circular dichroism and small-angle X-ray scattering of structure, self-organization, and stability of naïve Hsp60 in solution in comparison with bacterial GroEL. Experiments have been performed in different concentrations of guanidine hydrochloride, monitoring the dissociation of tetradecamers into heptamers and monomers, until unfolding. GroEL is proved to be more stable with respect to Hsp60, and the unfolding free energy as well as its dependence on denaturant concentration is obtained.
AB - Human Hsp60 chaperonin and its bacterial homolog GroEL, in association with the corresponding co-chaperonins Hsp10 and GroES, constitute important chaperone systems promoting the proper folding of several mitochondrial proteins. Hsp60 is also currently described as a ubiquitous molecule with multiple roles both in health conditions and in several diseases. Naïve Hsp60 bearing the mitochondrial import signal has been recently demonstrated to present different oligomeric organizations with respect to GroEL, suggesting new possible physiological functions. Here we present a combined investigation with circular dichroism and small-angle X-ray scattering of structure, self-organization, and stability of naïve Hsp60 in solution in comparison with bacterial GroEL. Experiments have been performed in different concentrations of guanidine hydrochloride, monitoring the dissociation of tetradecamers into heptamers and monomers, until unfolding. GroEL is proved to be more stable with respect to Hsp60, and the unfolding free energy as well as its dependence on denaturant concentration is obtained.
KW - CD
KW - Denaturation
KW - GroEL
KW - Guanidinium chloride
KW - Hsp60
KW - SAXS
UR - http://www.scopus.com/inward/record.url?scp=84948564151&partnerID=8YFLogxK
U2 - 10.1016/j.bpc.2015.07.006
DO - 10.1016/j.bpc.2015.07.006
M3 - Article
AN - SCOPUS:84948564151
SN - 0301-4622
VL - 208
SP - 68
EP - 75
JO - Biophysical Chemistry
JF - Biophysical Chemistry
ER -