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J. Biol. Chem., Vol. 269, Issue 37, 23045-23050, Sep, 1994
KJ Kaur and L Ruben
The following study examines the calmodulin (CaM) branch of the calcium
signal pathway in the protozoan parasite Trypanosoma brucei. To accomplish
this goal, a subset of cytosolic CaM-binding proteins (CaMBPs) was
partially purified by a combination of DE52 and CaM- Sepharose affinity
chromatography. Monoclonal antibodies (CBP-KK1) were used to clone the cDNA
for a 53-kDa CaMBP from a lambda ZAP expression library of the metacyclic
stage of T. brucei. The deduced amino acid sequence of clone CaMBP-12B had
81% overall amino acid identity to the translation elongation factor-1
alpha (EF-1 alpha) from Euglena gracilis and 76% identity to the rabbit
EF-1 alpha. Rabbit EF-1 alpha was recognized by CBP-KK1 and was shown to
bind to CaM-Sepharose in a calcium-dependent manner. By contrast, the
complex of EF-1 alpha beta gamma did not bind CaM-Sepharose. A
heterobifunctional sulfhydryl derivative of CaM (N-succinimidyl
3-(2-pyridyldithio)propionate-CaM) formed reducible cross-links with EF-1
alpha in solution but not with the complex of EF-1 alpha beta gamma.
Biotinylated CaM bound weakly to trypanosome and rabbit EF-1 alpha in a gel
overlay assay. This report demonstrates the direct interaction between CaM
and the translation elongation factor EF-1 alpha.
Protein translation elongation factor-1 alpha from Trypanosoma brucei binds calmodulin
Department of Biological Sciences, Southern Methodist University, Dallas, Texas 75275.
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