1. Identification, molecular and functional characterization of calmodulin gene of Phytomonas serpens 15T that shares high similarity with its pathogenic counterparts Trypanosoma cruzi.
- Author
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de Souza Tde A, Graça-de Souza VK, Lancheros CA, Monteiro-Góes V, Krieger MA, Goldenberg S, Yamauchi LM, and Yamada-Ogatta SF
- Subjects
- Amino Acid Motifs, Amino Acid Sequence, Calcium metabolism, Calmodulin genetics, Humans, Molecular Sequence Data, Protein Binding, Protein Structure, Secondary, Protozoan Proteins genetics, Sequence Alignment, Trypanosoma cruzi chemistry, Trypanosoma cruzi genetics, Trypanosoma cruzi metabolism, Trypanosomatina chemistry, Trypanosomatina metabolism, Calmodulin chemistry, Calmodulin metabolism, Cloning, Molecular, Protozoan Proteins chemistry, Protozoan Proteins metabolism, Trypanosomatina genetics
- Abstract
In trypanosomatids, Ca²+-binding proteins can affect parasite growth, differentiation and invasion. Due to their importance for parasite maintenance, they become an attractive target for drug discovery and design. Phytomonas serpens 15T is a non-human pathogenic trypanosomatid that expresses important protein homologs of human pathogenic trypanosomatids. In this study, the coding sequence of calmodulin, a Ca²+-binding protein, of P. serpens 15T was cloned and characterized. The encoded polypeptide (CaMP) displayed high amino acid identity to homolog protein of Trypanosoma cruzi and four helix-loop-helix motifs were found. CaMP sequence analysis showed 20 amino acid substitutions compared to its mammalian counterparts. This gene is located on a chromosomal band with estimated size of 1,300 kb and two transcripts were detected by Northern blot analysis. A polyclonal antiserum raised against the recombinant protein recognized a polypeptide with an estimated size of 17 kDa in log-phase promastigote extracts. The recombinant CaMP retains its Ca²+-binding capacity.
- Published
- 2011
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