Hsp90, a team player in protein quality control and the stress response in bacteria.
Microbiol Mol Biol Rev
; 88(2): e0017622, 2024 Jun 27.
Article
em En
| MEDLINE
| ID: mdl-38534118
ABSTRACT
SUMMARYHeat shock protein 90 (Hsp90) participates in proteostasis by facilitating protein folding, activation, disaggregation, prevention of aggregation, degradation, and protection against degradation of various cellular proteins. It is highly conserved from bacteria to humans. In bacteria, protein remodeling by Hsp90 involves collaboration with the Hsp70 molecular chaperone and Hsp70 cochaperones. In eukaryotes, protein folding by Hsp90 is more complex and involves collaboration with many Hsp90 cochaperones as well as Hsp70 and Hsp70 cochaperones. This review focuses primarily on bacterial Hsp90 and highlights similarities and differences between bacterial and eukaryotic Hsp90. Seminal research findings that elucidate the structure and the mechanisms of protein folding, disaggregation, and reactivation promoted by Hsp90 are discussed. Understanding the mechanisms of bacterial Hsp90 will provide fundamental insight into the more complex eukaryotic chaperone systems.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Bactérias
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Proteínas de Bactérias
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Dobramento de Proteína
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Proteínas de Choque Térmico HSP90
Limite:
Humans
Idioma:
En
Ano de publicação:
2024
Tipo de documento:
Article