Show simple item record

dc.creatorUZCANGA,GRACIELA
dc.creatorGALÁN-CARIDAD,JOSÉ MANUEL
dc.creatorSUAREZ,KAREM NORIS
dc.creatorBUBIS,JOSÉ
dc.date2003-01-01
dc.date.accessioned2019-05-02T21:21:12Z
dc.date.available2019-05-02T21:21:12Z
dc.identifierhttps://scielo.conicyt.cl/scielo.php?script=sci_arttext&pid=S0716-97602003000300008
dc.identifier.urihttp://revistaschilenas.uchile.cl/handle/2250/81480
dc.descriptionTrypanosoma cruzi epimastigotes were extracted under various conditions in order to examine the role of divalent cations in the solubilization of microtubule proteins. When epimastigotes were homogenized in the presence of 5 mM Mg+2 and 5 mM Ca+2, a protein kinase responsible for phosphorylating tubulin, as well as the tubulin that became phosphorylated, remained tightly associated with the parasite particulate and detergent-resistant fractions. On the contrary, tubulin kinase and its substrate were predominantly released into the parasite cytosolic and detergent-soluble fractions, when epimastigotes were extracted in the presence of 5 mM EDTA and 5 mM EGTA. These evidences demonstrated a divalent cation-dependent solubilization of the enzyme responsible for the phosphorylation of tubulin in T. cruzi epimastigotes and suggested a tight association between tubulin and this kinase. Under all conditions tested, tubulin kinase activity in epimastigote extracts was lower than the addition of the corresponding value in the parasite cytosolic and membranous fractions, suggesting the presence of a kinase inhibitor or regulatory subunit which also seemed to be modulated by divalent cations. Additionally, inhibition experiments in the presence of heparin, 2,3-bisphosphoglycerate and GTP established that the parasite tubulin kinase corresponded to a protein kinase CK2
dc.formattext/html
dc.languageen
dc.publisherSociedad de Biología de Chile
dc.relation10.4067/S0716-97602003000300008
dc.rightsinfo:eu-repo/semantics/openAccess
dc.sourceBiological Research v.36 n.3-4 2003
dc.subjectmicrotubules
dc.subjectpost-translational modification of tubulin
dc.subjectprotein kinase CK2
dc.subjectprotein phosphorylation-dephosphorylation
dc.subjectsignal transduction
dc.subjectTrypanosoma cruzi
dc.subjecttubulin
dc.titleDivalent cation hinder the solubilization of a tubulin kinase activity from Trypanosoma cruzi epimastigotes


This item appears in the following Collection(s)

Show simple item record