Search results for " GroEL"

Multilocus typing for characterization of ‘Candidatus Phytoplasma asteris’-related strains in several ornamental species in Italy

2018

Different ornamental plants showing symptoms referable to phytoplasma presence and collected between 1993 and 2015 in various floricultural areas in north and south of Italy, enclosing Sicily, resulted to be infected by ‘Candidatus Phytoplasma asteris’-related strains, and after PCR/RFLP identification on 16Sr gene were assigned to 16SrI-B subgroup. These infected samples were employed for phytoplasma strain differentiation on tuf, groel, rp and amp genes. In particular, the 23 phytoplasma strains employed were from hydrangea (5), primula (3), gentian (2), petunia (2) and gerbera (1) samples showing flower virescence; from gladiolus samples both in vivo and in micropropagation (2) showing t…

Chaperonin of Group I: Oligomeric spectrum and biochemical and biological implications

2018

Chaperonins play various physiological roles and can also be pathogenic. Elucidation of their structure, e.g., oligomeric status and post-translational modifications (PTM), is necessary to understand their functions and mechanisms of action in health and disease. Group I chaperonins form tetradecamers with two stacked heptameric rings. The tetradecamer is considered the typical functional complex for folding of client polypeptides. However, other forms such as the monomer and oligomers with smaller number of subunits than the classical tetradecamer, also occur in cells. The properties and functions of the monomer and oligomers, and their roles in chaperonin-associated diseases are still inc…

Naïve Hsp60, similarly to GroEL, oligomerizes to build heptameric and tetradecameric structures.

2013

Hsp60 chaperonopathies and chaperonotherapy: targets and agents

2014

Hsp60 (Cpn60) assembles into a tetradecamer that interacts with the co-chaperonin Hsp10 (Cpn10) to assist client polypeptides to fold, but it also has other roles, including participation in pathogenic mechanisms.Hsp60 chaperonopathies are pathological conditions, inherited or acquired, in which the chaperone plays a determinant etiologic-pathogenic role. These diseases justify selection of Hsp60 as a target for developing agents that interfere with its pathogenic effects. We provide information on how to proceed.The information available encourages the development of ways to improve Hsp60 activity (positive chaperonotherapy) when deficient or to block it (negative chaperonotherapy) when pa…

Stability and disassembly properties of human naïve Hsp60 and bacterial GroEL chaperonins.

2015

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 sta…