Low-temperature features of the psychrophilic chaperonin from Pseudoalteromonas haloplanktis.
Arch Microbiol
; 206(7): 299, 2024 Jun 11.
Article
em En
| MEDLINE
| ID: mdl-38861015
ABSTRACT
Chaperonins from psychrophilic bacteria have been shown to exist as single-ring complexes. This deviation from the standard double-ring structure has been thought to be a beneficial adaptation to the cold environment. Here we show that Cpn60 from the psychrophile Pseudoalteromonas haloplanktis (Ph) maintains its double-ring structure also in the cold. A strongly reduced ATPase activity keeps the chaperonin in an energy-saving dormant state, until binding of client protein activates it. Ph Cpn60 in complex with co-chaperonin Ph Cpn10 efficiently assists in protein folding up to 55 °C. Moreover, we show that recombinant expression of Ph Cpn60 can provide its host Escherichia coli with improved viability under low temperature growth conditions. These properties of the Ph chaperonin may make it a valuable tool in the folding and stabilization of psychrophilic proteins.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Dobramento de Proteína
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Temperatura Baixa
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Pseudoalteromonas
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Escherichia coli
Idioma:
En
Revista:
Arch Microbiol
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
Alemanha