@article{fdi:010037791,
  title = {{P}roof of interaction between {L}eishmania {SIR}2{RP}1 deacetylase and chaperone {HSP}83},
  author = {{M}onte-{A}legre, {A}driano and {V}ergnes, {B}aptiste and {P}oncet, {J}. and {M}athieu-{D}aude, {F}ran{\c{c}}oise and da {S}ilva, {A}. {C}. and {O}uaissi, {A}li and {S}ereno, {D}enis},
  editor = {},
  language = {{ENG}},
  abstract = {{T}he cytoplasmic {L}eishmania silent information regulator 2 ({SIR}2){RP}1 protein is essential for parasite growth and survival and constitutes an attractive therapeutic target. {L}ittle 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. {W}e carried out co-immunoprecipitation experiments on the soluble fractions of wild-type and parasites overexpressing {L}m{SIR}2{RP}1 and found that the essential chaperone heat shock protein ({HSP}) 83, the {L}eishmania ortholog of the mammalian {HSP}90, constantly co-immunoprecipitated with {L}m{SIR}2{RP}1. {W}e found that {L}eishmania {HSP}83 is among the lysine acetylated protein, but the intracellular level of {SIR}2{RP}1 does not influence the acetylation status of {HSP}83. {F}inally, the modified {G}eldanamycin susceptibility (an inhibitor of {HSP}83) exhibited by {SIR}2{RP}1 mutant parasites support an in vivo relationship between the chaperone activity of {HSP}83 and {L}m{SIR}2{RP}1. {A}n insight on the nature of the interaction in {L}eishmania is required to understand its role in the cell fate control during cytodifferentiation.},
  keywords = {},
  booktitle = {},
  journal = {{P}arasitology {R}esearch},
  volume = {100},
  numero = {4},
  pages = {811--818},
  ISSN = {0932-0113},
  year = {2007},
  DOI = {10.1007/s00436-006-0352-3},
  URL = {https://www.documentation.ird.fr/hor/fdi:010037791},
}