Monte-Alegre Adriano auteur aut IRD Vergnes Baptiste auteur aut IRD Poncet J. auteur aut IRD Mathieu-Daude Françoise auteur aut IRD da Silva A. C. auteur aut IRD Ouaissi Ali auteur aut IRD Sereno Denis auteur aut IRD text journalArticle eng text/pdf born digital access The cytoplasmic Leishmania silent information regulator 2 (SIR2)RP1 protein is essential for parasite growth and survival and constitutes an attractive therapeutic target. Little information is available on putative substrate(s) and/or partner(s) that could shed light on the pathways in which this enzyme plays a role. We carried out co-immunoprecipitation experiments on the soluble fractions of wild-type and parasites overexpressing LmSIR2RP1 and found that the essential chaperone heat shock protein (HSP) 83, the Leishmania ortholog of the mammalian HSP90, constantly co-immunoprecipitated with LmSIR2RP1. We found that Leishmania HSP83 is among the lysine acetylated protein, but the intracellular level of SIR2RP1 does not influence the acetylation status of HSP83. Finally, the modified Geldanamycin susceptibility (an inhibitor of HSP83) exhibited by SIR2RP1 mutant parasites support an in vivo relationship between the chaperone activity of HSP83 and LmSIR2RP1. An insight on the nature of the interaction in Leishmania is required to understand its role in the cell fate control during cytodifferentiation. specialized 052 100 4 811-818 2007 0932-0113 https://www.documentation.ird.fr/hor/fdi:010037791 10.1007/s00436-006-0352-3 0932-0113 [F A010037791] https://www.documentation.ird.fr/hor/fdi:010037791 https://www.documentation.ird.fr/intranet/publi/2007/03/010037791.pdf Accès réservé (Intranet de l'IRD) IRD - Base Horizon / Pleins textes 2007-03-30 2017-08-23 fdi:010037791 fre