The Trypanosoma cruzi nucleic acid binding protein Tc38 presents changes in the intramitochondrial distribution during the cell cycle

The Trypanosoma cruzi nucleic acid binding protein Tc38 presents changes in the intramitochondrial distribution during the cell cycle

Author Duhagon, Maria A. Google Scholar
Pastro, Lucia Google Scholar
Sotelo-Silveira, Jose R. Google Scholar
Perez-Diaz, Leticia Google Scholar
Maugeri, Dante Google Scholar
Nardelli, Sheila Cristina Autor UNIFESP Google Scholar
Schenkman, Sergio Autor UNIFESP Google Scholar
Williams, Noreen Google Scholar
Dallagiovanna, Bruno Google Scholar
Garat, Beatriz Google Scholar
Institution Fac Ciencias
Fac Med
Inst Invest Biol Clemente Estable Montevideo Urug
Univ Nacl Gen San Martin
Universidade Federal de São Paulo (UNIFESP)
SUNY Buffalo
Inst Biol Mol Parana
Abstract Background: Tc38 of Trypanosoma cruzi has been isolated as a single stranded DNA binding protein with high specificity for the poly [dT-dG] sequence. It is present only in Kinetoplastidae protozoa and its sequence lacks homology to known functional domains. Tc38 orthologues present in Trypanosoma brucei and Leishmania were proposed to participate in quite different cellular processes. To further understand the function of this protein in Trypanosoma cruzi, we examined its in vitro binding to biologically relevant [dT-dG] enriched sequences, its expression and subcellular localization during the cell cycle and through the parasite life stages.Results: By using specific antibodies, we found that Tc38 protein from epimastigote extracts participates in complexes with the poly [dT-dG] probe as well as with the universal minicircle sequence (UMS), a related repeated sequence found in maxicircle DNA, and the telomeric repeat. However, we found that Tc38 predominantly localizes into the mitochondrion. Though Tc38 is constitutively expressed through non-replicating and replicating life stages of T. cruzi, its subcellular localization in the unique parasite mitochondrion changes according to the cell cycle stage. in epimastigotes, Tc38 is found only in association with kDNA in G1 phase. From the S to G2 phase the protein localizes in two defined and connected spots flanking the kDNA. These spots disappear in late G2 turning into a diffuse dotted signal which extends beyond the kinetoplast. This later pattern is more evident in mitosis and cytokinesis. Finally, late in cytokinesis Tc38 reacquires its association with the kinetoplast. in non-replicating parasite stages such as trypomastigotes, the protein is found only surrounding the entire kinetoplast structure.Conclusions: the dynamics of Tc38 subcellular localization observed during the cell cycle and life stages support a major role for Tc38 related to kDNA replication and maintenance.
Language English
Sponsor FIRCA
Fondo Clemente Estable (DICyT)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Grant number FIRCA: R03 TW05665-01
Fondo Clemente Estable (DICyT): 7109
Date 2009-02-11
Published in Bmc Microbiology. London: Biomed Central Ltd, v. 9, 11 p., 2009.
ISSN 1471-2180 (Sherpa/Romeo, impact factor)
Publisher Biomed Central Ltd
Extent 11
Access rights Open access Open Access
Type Article
Web of Science ID WOS:000264160400002

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