| Autor: |
de Souza Tde A; Departamento de Microbiologia, Centro de Ciências Biológicas, Universidade Estadual de Londrina, Rodovia Celso Garcia Cid, PR 445, Km 380, Londrina, Paraná CEP 86051-980, Brazil., Graça-de Souza VK, Lancheros CA, Monteiro-Góes V, Krieger MA, Goldenberg S, Yamauchi LM, Yamada-Ogatta SF |
| Jazyk: |
angličtina |
| Zdroj: |
The protein journal [Protein J] 2011 Mar; Vol. 30 (3), pp. 212-9. |
| DOI: |
10.1007/s10930-011-9322-4 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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