Protein–protein interaction map of the Trypanosoma cruzi ribosomal P protein complex

The large subunit of the eukaryotic ribosome possesses a long and protruding stalk formed by the ribosomal P proteins. Four out of five ribosomal P proteins of Trypanosoma cruzi, TcP0, TcP1alpha, TcP2alpha, and TcP2beta had been previously characterized. Data mining of the T. cruzi genome data base...

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Detalles Bibliográficos
Autores: Juri Ayub, Maximiliano, Smulski, Cristian Roberto, Nyambega, Benson, Bercovich, Natalia, Masiga, Dan, Vazquez, Martin Pablo, Aguilar, Carlos Fernando, Levin, Mariano Jorge
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2005
País:Argentina
Institución:Consejo Nacional de Investigaciones Científicas y Técnicas
Repositorio:CONICET Digital (CONICET)
Idioma:inglés
OAI Identifier:oai:ri.conicet.gov.ar:11336/44590
Acceso en línea:http://hdl.handle.net/11336/44590
Access Level:acceso abierto
Palabra clave:Trypanosoma Cruzi
Ribosome
Ribosomal P Protein
Yeast Two-Hybrid
https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
Descripción
Sumario:The large subunit of the eukaryotic ribosome possesses a long and protruding stalk formed by the ribosomal P proteins. Four out of five ribosomal P proteins of Trypanosoma cruzi, TcP0, TcP1alpha, TcP2alpha, and TcP2beta had been previously characterized. Data mining of the T. cruzi genome data base allowed the identification of the fifth member of this protein group, a novel P1 protein, named P1beta. To gain insight into the assembly of the stalk, a yeast two-hybrid based protein interaction map was generated. A parasite specific profile of interactions amongst the ribosomal P proteins of T. cruzi was evident. The TcP0 protein was able to interact with all both P1 and both P2 proteins. Moreover, the interactions between P2beta with P1alpha as well as with P2alpha were detected, as well as the ability of TcP2beta to homodimerize. A quantitative evaluation of the interactions established that the strongest interacting pair was TcP0-TcP1beta.