Tubulin is hyperphosphorylated on serine and tyrosine residues in arsenite-resistant Leishmania donovani promastigotes.
An arsenite-resistant strain of Leishmania donovani was generated in vitro by the sequential exposure of a wild type strain to increasing concentrations of sodium m-arsenite. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of whole cell lysates of the two strains revealed that a protein band at the 55 kDa position showed slower migration in the resistant samples. This band was identified as tubulin by immunoblotting, with both alpha- and beta-tubulin showing retarded migration in the resistant strain. Investigations into the reason for the observed slower migration revealed that phosphorylation of tubulin on both serine and tyrosine residues was enhanced in the resistant strain when compared to the wild type strain.
Prasad
V
V
Department of Biotechnology, National Institute of Pharmaceutical Education and Research, Punjab, India.
Dey
C S
CS
D000818:Animals; D018053:Arsenites / Q000494:pharmacology*; D003470:Culture Media; D004351:Drug Resistance; D004591:Electrophoresis, Polyacrylamide Gel; D007893:Leishmania donovani / Q000187:drug effects* / Q000254:growth & development / Q000378:metabolism; D010766:Phosphorylation; D012694:Serine / Q000378:metabolism; D014404:Tubulin / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism
D018053:Arsenites; D003470:Culture Media; D014404:Tubulin; D014443:Tyrosine; D012694:Serine