INVESTIGADORES
COCERES Veronica Mabel
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 AND CORVI MM
Lugar:
Provincia de Tucumán
Reunión:
Congreso; XLV Reunión Anual Sociedad Argentina de Investigación Bioquímica y Biología Molecular; 2009
Institución organizadora:
Sociedad Argentina de Investigación Bioquímica y Biología Molecular
Resumen:
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 membrane complex. TgHSP20 displays a behavior similar to an integral membrane protein, since this localization is not altered by incubation with high salt concentrations. TgHSP20 is predicted to be palmitoytlated. 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.
