Trypanosoma cruzi epimastigote forms possess a Ca2+‐calmodulin dependent protein kinase

FEBS Letters

Solari, A.¹  Ogueta, S.B.²  Téllez-Iñón, M.T.² 

[1] Facultad de Ciencias Medicos, UBA, Paraguay 2155, 1121 Buenos Aires, Argentina;Instituto de Investigations en Ingenieria Genética γ Biologia Molecular (INGEBI) and Facultad de Ciencias Exactas γ Naturales, UBA, Vuelta de Obllgado 2490, 1428 Buenos Aires, Argentina

关键词: Ca2+-calmodulin protein kinase;    Cytoskeleton;    Flagella;    Trypanosoma cruzi;    Trypanosomatid;    ATP;    adenosine 5'-triphosphate;    βME;    β-mercaptoethanol;    cAMP;    cyclic adenosine monophosphate;    CaM;    calmodulin;    CaM kinase II;    Ca2+-calmodulin-dependent protein kinase type II;    DTT;    d;    l-dithiothreitol;    E64 trans-epoxysuccinyl-l-leucylamido (4-guanidino) butane;    EDTA;    ethylendiaminetetraacetic acid;    EGTA;    ethylene glycol-bis(β-amino-ethylether);    PMSF;    phenylmethyl-sulfonyl fluoride;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    TLCK;    Nα-p-tosyl-l-lysine chloro-methyl ketone;   

DOI  :  10.1016/0014-5793(94)80212-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Trypanosoma cruzi epimastigote forms showed a tightly bound Ca²⁺-calmodulin-dependent protein kinase activity, which could be partially extracted from membranes and axonemes. The enzyme is constituted by subunits which were autophosphorylated in the absence of exogenous substrates. An antibody against CaM kinase II recognized a Ca²⁺- or Ca²⁺-CaM-dependent conformational epitope in these fractions. The detected bands were of molecular weights similar to the α and β subunits of the corresponding bovine brain enzyme (60 and 50 kDa). Studies using [¹²⁵I]CaM revealed the presence of a CaM-binding domain. These experiments confirm that the parasite possesses a paniculate CaM kinase with characteristics similar to the bovine brain enzyme.

【 授权许可】

Unknown