Tubulin is hyperphosphorylated on serine and tyrosine residues in arsenite-resistant Leishmania donovani promastigotes

Authors
Citation
V. Prasad et Cs. Dey, Tubulin is hyperphosphorylated on serine and tyrosine residues in arsenite-resistant Leishmania donovani promastigotes, PARASIT RES, 86(11), 2000, pp. 876-880
Citations number
32
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Microbiology
Journal title
PARASITOLOGY RESEARCH
ISSN journal
0932-0113 → ACNP
Volume
86
Issue
11
Year of publication
2000
Pages
876 - 880
Database
ISI
SICI code
0932-0113(200011)86:11<876:TIHOSA>2.0.ZU;2-N
Abstract
An arsenite-resistant strain of Leishmania donovani was generated in vitro by the sequential exposure of a wild type strain to increasing concentratio ns of sodium m-arsenite. Sodium dodecyl sulfate-polyacrylamide gel electrop horesis analysis of whole cell lysates of the two strains revealed that a p rotein 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 e nhanced in the resistant strain when compared to the wild type strain.