Toxoplasma gondii: a bradyzoite-specific DnaK-tetratricopeptide repeat (DnaK-TPR) protein interacts with p23 co-chaperone protein.
Exp Parasitol
; 127(4): 795-803, 2011 Apr.
Article
em En
| MEDLINE
| ID: mdl-21281637
ABSTRACT
The DnaK-tetratricopeptide repeat (DnaK-TPR) gene (ToxoDB ID, TGME49_002020) is expressed predominantly at the bradyzoite stage. DnaK-TPR protein has a heat shock protein (DnaK) and tetratricopeptide repeat (TPR) domains with amino acid sequence similarity to the counterparts of other organisms (40.2-43.7% to DnaK domain and 41.1-66.0% to TPR domain). These findings allowed us to infer that DnaK-TPR protein is important in the tachyzoite-to-bradyzoite development or maintenance of cyst structure although the function of this gene is still unknown. An immunofluorescence assay (IFA) revealed that DnaK-TPR protein was expressed in Toxoplasma gondii-encysted and in vitro-induced bradyzoites and distributed in the whole part of parasite cells. We conducted yeast two-hybrid screening to identify proteins interacting with DnaK-TPR protein, and demonstrated that DnaK-TPR protein interacts with p23 co-chaperone protein (Tgp23). It was expected that DnaK-TPR protein would have a function as a molecular chaperon in bradyzoite cells associated with Tgp23. Possible mechanisms for this gene are discussed.
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Base de dados:
MEDLINE
Assunto principal:
Toxoplasma
/
Proteínas de Protozoários
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Chaperonas Moleculares
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Domínios e Motivos de Interação entre Proteínas
Tipo de estudo:
Prognostic_studies
Limite:
Animals
/
Female
/
Humans
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Male
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article