Isolation and characterization of a unique 15 kilodalton trypanosome subpellicular microtubule-associated protein.
A protein of 15 kDa (p15) was isolated from Trypanosoma brucei subpellicular microtubules by tubulin affinity chromatography. The protein bound tubulin specifically both in its native form and after SDS-PAGE in tubulin overlay experiments. p15 promoted both the in vitro polymerization of purified calf brain tubulin and the bundling of preformed mammalian microtubules. Immunolabeling identified p15 at multiple sites along microtubule polymers comprising calf brain tubulin and p15 as well as on the subpellicular microtubules of cryosectioned trypanosomes. Antibodies directed against p15 did not cross react with mammalian microtubules. It is suggested that p15 is a trypanosome-specific microtubule-associated protein (MAP) that contributes to the unique organization of the subpellicular microtubules.
Balaban
N
N
Department of Membrane Research, Weizmann Institute of Science, Rehovot, Israel.
Goldman
R
R
D000818:Animals; D001667:Binding, Competitive; D002846:Chromatography, Affinity; D007150:Immunohistochemistry; D008869:Microtubule-Associated Proteins / Q000302:isolation & purification* / Q000378:metabolism; D008870:Microtubules / Q000737:chemistry* / Q000648:ultrastructure; D008970:Molecular Weight; D014346:Trypanosoma brucei brucei / Q000737:chemistry* / Q000648:ultrastructure; D014404:Tubulin / Q000378:metabolism
D008869:Microtubule-Associated Proteins; D014404:Tubulin