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

被引：15

作者：

Prasad, V ^{[1
]}

Dey, CS ^{[1
]}

机构：

[1] Natl Inst Pharmaceut Educ & Res, Dept Biotechnol, SAS Nagar 160062, Punjab, India

来源：

PARASITOLOGY RESEARCH | 2000年 / 86卷 / 11期

关键词：

D O I：

10.1007/s004360000249

中图分类号：

R38 [医学寄生虫学]; Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ; 100103 ;

摘要：

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.

引用

页码：876 / 880

页数：5