Protein translation elongation factor-1α from Trypanosoma brucei binds calmodulin

Kiran J. Kaur, Larry Ruben

Research output: Contribution to journalArticle

69 Scopus citations

Abstract

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 λZAP 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-1α (EF-1α) from Euglena gracilis and 76% identity to the rabbit EF-1α. Rabbit EF-1α was recognized by CBP-KK1 and was shown to bind to CaM-Sepharose in a calcium-dependent manner. By contrast, the complex of EF-1αβγ did not bind CaM-Sepharose. A heterobifunctional sulfhydryl derivative of CaM (N-succinimydyl 3-(2- pyridyldithio)propionate-CaM) formed reducible cross-links with EF-1α in solution but not with the complex of EF-1αβγ. Biotinylated CaM bound weakly to trypanosome and rabbit EF-1α in a gel overlay assay. This report demonstrates the direct interaction between CaM and the translation elongation factor EF-1α.

Original languageEnglish (US)
Pages (from-to)23045-23050
Number of pages6
JournalJournal of Biological Chemistry
Volume269
Issue number37
StatePublished - Sep 16 1994

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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