Article ; Online: Oligomeric State and Holding Activity of Hsp60.
International journal of molecular sciences
2023 Volume 24, Issue 9
Abstract: Similar to its bacterial homolog GroEL, Hsp60 in oligomeric conformation is known to work as a folding machine, with the assistance of co-chaperonin Hsp10 and ATP. However, recent results have evidenced that Hsp60 can stabilize aggregation-prone ... ...
Abstract | Similar to its bacterial homolog GroEL, Hsp60 in oligomeric conformation is known to work as a folding machine, with the assistance of co-chaperonin Hsp10 and ATP. However, recent results have evidenced that Hsp60 can stabilize aggregation-prone molecules in the absence of Hsp10 and ATP by a different, "holding-like" mechanism. Here, we investigated the relationship between the oligomeric conformation of Hsp60 and its ability to inhibit fibrillization of the Ab40 peptide. The monomeric or tetradecameric form of the protein was isolated, and its effect on beta-amyloid aggregation was separately tested. The structural stability of the two forms of Hsp60 was also investigated using differential scanning calorimetry (DSC), light scattering, and circular dichroism. The results showed that the protein in monomeric form is less stable, but more effective against amyloid fibrillization. This greater functionality is attributed to the disordered nature of the domains involved in subunit contacts. |
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MeSH term(s) | Chaperonin 60/metabolism ; Adenosine Triphosphate/metabolism ; Chaperonin 10/chemistry ; Protein Folding |
Chemical Substances | Chaperonin 60 ; Adenosine Triphosphate (8L70Q75FXE) ; Chaperonin 10 |
Language | English |
Publishing date | 2023-04-25 |
Publishing country | Switzerland |
Document type | Journal Article |
ZDB-ID | 2019364-6 |
ISSN | 1422-0067 ; 1422-0067 ; 1661-6596 |
ISSN (online) | 1422-0067 |
ISSN | 1422-0067 ; 1661-6596 |
DOI | 10.3390/ijms24097847 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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