The Trypanosoma cruzi nucleic acid binding protein Tc38 presents changes in the intramitochondrial distribution during the cell cycle
Autor(a) principal: | |
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Data de Publicação: | 2009 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://dx.doi.org/10.1186/1471-2180-9-34 http://repositorio.unifesp.br/handle/11600/31317 |
Resumo: | 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. |
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The Trypanosoma cruzi nucleic acid binding protein Tc38 presents changes in the intramitochondrial distribution during the cell cycleBackground: 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.Fac Ciencias, Lab Interacc Mol, Montevideo, UruguayFac Med, Dept Genet, Montevideo, UruguayFac Ciencias, Dept Biol Celular & Mol, Montevideo, UruguayInst Invest Biol Clemente Estable Montevideo Urug, Dept Neurobiol Celular & Mol, Montevideo, UruguayUniv Nacl Gen San Martin, CONICET, INTECH, Inst Invest Biotecnol, Buenos Aires, DF, ArgentinaUniversidade Federal de São Paulo, Dept Microbiol Imunol & Parasitol, São Paulo, BrazilSUNY Buffalo, Dept Microbiol & Immunol, Buffalo, NY 14260 USAInst Biol Mol Parana, Curitiba, Parana, BrazilUniversidade Federal de São Paulo, Dept Microbiol Imunol & Parasitol, São Paulo, BrazilWeb of ScienceFIRCAFondo Clemente Estable (DICyT)FAPESConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)PROSULPEDECIBAAMSUD-PasteurFIRCA: R03 TW05665-01Fondo Clemente Estable (DICyT): 7109Biomed Central LtdFac CienciasFac MedInst Invest Biol Clemente Estable Montevideo UrugUniv Nacl Gen San MartinUniversidade Federal de São Paulo (UNIFESP)SUNY BuffaloInst Biol Mol ParanaDuhagon, Maria A.Pastro, LuciaSotelo-Silveira, Jose R.Perez-Diaz, LeticiaMaugeri, DanteNardelli, Sheila Cristina [UNIFESP]Schenkman, Sergio [UNIFESP]Williams, NoreenDallagiovanna, BrunoGarat, Beatriz2016-01-24T13:52:16Z2016-01-24T13:52:16Z2009-02-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion11application/pdfhttp://dx.doi.org/10.1186/1471-2180-9-34Bmc Microbiology. London: Biomed Central Ltd, v. 9, 11 p., 2009.10.1186/1471-2180-9-34WOS000264160400002.pdf1471-2180http://repositorio.unifesp.br/handle/11600/31317WOS:000264160400002engBmc Microbiologyinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESP2024-08-07T17:05:53Zoai:repositorio.unifesp.br/:11600/31317Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestbiblioteca.csp@unifesp.bropendoar:34652024-08-07T17:05:53Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.none.fl_str_mv |
The Trypanosoma cruzi nucleic acid binding protein Tc38 presents changes in the intramitochondrial distribution during the cell cycle |
title |
The Trypanosoma cruzi nucleic acid binding protein Tc38 presents changes in the intramitochondrial distribution during the cell cycle |
spellingShingle |
The Trypanosoma cruzi nucleic acid binding protein Tc38 presents changes in the intramitochondrial distribution during the cell cycle Duhagon, Maria A. |
title_short |
The Trypanosoma cruzi nucleic acid binding protein Tc38 presents changes in the intramitochondrial distribution during the cell cycle |
title_full |
The Trypanosoma cruzi nucleic acid binding protein Tc38 presents changes in the intramitochondrial distribution during the cell cycle |
title_fullStr |
The Trypanosoma cruzi nucleic acid binding protein Tc38 presents changes in the intramitochondrial distribution during the cell cycle |
title_full_unstemmed |
The Trypanosoma cruzi nucleic acid binding protein Tc38 presents changes in the intramitochondrial distribution during the cell cycle |
title_sort |
The Trypanosoma cruzi nucleic acid binding protein Tc38 presents changes in the intramitochondrial distribution during the cell cycle |
author |
Duhagon, Maria A. |
author_facet |
Duhagon, Maria A. Pastro, Lucia Sotelo-Silveira, Jose R. Perez-Diaz, Leticia Maugeri, Dante Nardelli, Sheila Cristina [UNIFESP] Schenkman, Sergio [UNIFESP] Williams, Noreen Dallagiovanna, Bruno Garat, Beatriz |
author_role |
author |
author2 |
Pastro, Lucia Sotelo-Silveira, Jose R. Perez-Diaz, Leticia Maugeri, Dante Nardelli, Sheila Cristina [UNIFESP] Schenkman, Sergio [UNIFESP] Williams, Noreen Dallagiovanna, Bruno Garat, Beatriz |
author2_role |
author author author author author author author author author |
dc.contributor.none.fl_str_mv |
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 |
dc.contributor.author.fl_str_mv |
Duhagon, Maria A. Pastro, Lucia Sotelo-Silveira, Jose R. Perez-Diaz, Leticia Maugeri, Dante Nardelli, Sheila Cristina [UNIFESP] Schenkman, Sergio [UNIFESP] Williams, Noreen Dallagiovanna, Bruno Garat, Beatriz |
description |
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. |
publishDate |
2009 |
dc.date.none.fl_str_mv |
2009-02-11 2016-01-24T13:52:16Z 2016-01-24T13:52:16Z |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1186/1471-2180-9-34 Bmc Microbiology. London: Biomed Central Ltd, v. 9, 11 p., 2009. 10.1186/1471-2180-9-34 WOS000264160400002.pdf 1471-2180 http://repositorio.unifesp.br/handle/11600/31317 WOS:000264160400002 |
url |
http://dx.doi.org/10.1186/1471-2180-9-34 http://repositorio.unifesp.br/handle/11600/31317 |
identifier_str_mv |
Bmc Microbiology. London: Biomed Central Ltd, v. 9, 11 p., 2009. 10.1186/1471-2180-9-34 WOS000264160400002.pdf 1471-2180 WOS:000264160400002 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Bmc Microbiology |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
11 application/pdf |
dc.publisher.none.fl_str_mv |
Biomed Central Ltd |
publisher.none.fl_str_mv |
Biomed Central Ltd |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
biblioteca.csp@unifesp.br |
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1814268404722302976 |