Proof of interaction between Leishmania SIR2RP1 deacetylase and chaperone HSP83

• Type: Article in International Scientific Journal
• Date: 2007

Authors

Monte-Alegre Adriano (Author) Other; Baptiste Vergnes (Author) Other; Joel Poncet (Author) Other; Anabela Cordeiro da Silva (Author) FFUP; Ali Ouaissi (Author) Other; Denis Sereno (Author) Other

Journal

Title: Parasitology Research

Vol. 100 No. 4

Pages: 811-818

ISSN: 0932-0113

Publisher: Springer Nature

Indexing

ISI Web of Knowledge - 10 Citations

ISI Web of Science

Scopus - 9 Citations

Scientific classification

FOS: Medical and Health sciences > Other medical sciences

CORDIS: Health sciences

Other information

Authenticus ID: P-004-BN5

Resumo (PT): 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 coimmunoprecipitation 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. <br> <br> <a target="_blank" href="http://www.springerlink.com/content/jg005u19p3564844/?p=a4ea080560fe476b82c49f780b15591a&pi=21"> Texto integral</a> <br> <br>

Abstract (EN): 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 coimmunoprecipitation 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. <br> <br> <a target="_blank" href="http://www.springerlink.com/content/jg005u19p3564844/?p=a4ea080560fe476b82c49f780b15591a&pi=21"> Full text</a> <br> <br>

Language: Portuguese

Type (Professor's evaluation): Scientific