INVESTIGADORES
CORVI Maria Martha
congresos y reuniones científicas
Título:
The small heat shock protein 20 is palmitoylated ?in vivo? in Toxoplasma gondii
Autor/es:
DE NAPOLI, MG; COCERES, VM; NIETO GUIL, AF; ANGEL, SO; CORVI, MM
Lugar:
San Miguel de Tucuman
Reunión:
Congreso; XLV Reunion Anual de la Sociedad Argentina de Investigaciones Bioquimicas y Biologia Molecular; 2009
Resumen:
The small heat shock protein 20 is palmitoylated ?in vivo? in Toxoplasma gondii De Napoli MG, Coceres VM, Nieto Guil AF, Angel SO and Corvi MM. Laboratorio de parasitologia molecular. IIB-INTECH. Chascomús, provincia de Buenos Aires, Argentina The small heat shock protein 20 in Toxoplasma gondii (TgHSP20) does not contain any transmembrane domain or hydrophobic regions. However, it is localized to the plasma membrane and to the inner membrane complex. TgHSP20 displays a behavior similar to an integral membrane protein, since this localization is not altered by incubation with high salt concentrations. In fact, membrane localization is only altered by treatment with detergents. TgHSP20 was predicted to be palmitoylated by ?in silico? analysis. Palmitoylation is the post-translational attachment of palmitate to cysteine residues of a protein. This modification plays a critical role in the localization and activity of the protein that is modified. Metabolically labeled parasites showed that TgHSP20 is palmitoylated ?in vivo?. Mutation of candidate cysteine residues revealed that palmitoylation plays a critical role in TgHSP20 localization. Studies on the importance of this modification in the biology of T. gondii are being carried out.