DE MIGUEL Natalia
Toxoplasma gondii Sis1-like J-domain protein is a cytosolic chaperone associated to HSP90/HSP70 complex
MARIA J. FIGUERAS; OSVALDO A. MARTIN; PABLO C. ECHEVERRIA; NATALIA DE MIGUEL; ARUNASALAM NAGULESWARAN; WILLIAM J. SULLIVAN JR.; MARIA M. CORVI; SERGIO O. ANGEL
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
ELSEVIER SCIENCE BV
Año: 2012 vol. 50 p. 725 - 733
Toxoplasma gondii is an obligate intracellular protozoan parasite in which 36 predicted Hsp40 family members were identified by searching the T. gondii genome. The predicted protein sequence from the gene ID TGME49_065310 showed an amino acid sequence and domain structure similar to Saccharomyces cerevisiae Sis1. TgSis1 did not show differences in its expression profile during alkaline stress by microarray analysis. Furthermore, TgSis1 showed to be a cytosolic Hsp40 which co-immunoprecipitated with T. gondii Hsp70 and Hsp90. Structural modeling of the TgSis1 peptide binding fragment revealed structural and electrostatic properties different from the experimental model of human Sis1-like protein (Hdj1). Based on these differences; we propose that TgSis1 may be a potentially attractive drug target for developing a novel anti-T. gondii therapy.