Characterization of a Trypanosoma cruzi acetyltransferase: cellular location, activity and structure

Autores
Ochaya, Stephen; Respuela, Patricia; Simonsson, Maria; Saraswathi, Abhiman; Branche, Carole; Lee, Jennifer; Bua, Jacqueline; Nilsson, Daniel; Åslund, Lena; Bontempi, Esteban; Andersson, Björn
Año de publicación
2007
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Ochaya, Stephen. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
Fil: Respuela, Patricia. Rudbeck Laboratory. Department of Genetics and Pathology; Suecia.
Fil: Simonsson, Maria. Ludwig Institute for Cancer Research; Suecia.
Fil: Saraswathi, Abhiman. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
Fil: Branche, Carole. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
Fil: Lee, Jennifer. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
Fil: Bua, Jacqueline. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
Fil: Nilsson, Daniel. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
Fil: Åslund, Lena. Rudbeck Laboratory. Department of Genetics and Pathology; Suecia.
Fil: Bontempi, Esteban. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
Fil: Andersson, Björn. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
Trypanosomatids are widespread parasites that cause three major tropical diseases. In trypanosomatids, as in most other organisms, acetylation is a common protein modification that is important in multiple, diverse processes. This paper describes a new member of the Trypanosoma cruzi acetyltransferase family. The gene is single copy and orthologs are also present in the other two sequenced trypanosomatids, Trypanosoma brucei and Leishmania major. This protein (TcAT-1) has the essential motifs present in members of the GCN5-related acetyltransferase (GNAT) family, as well as an additional motif also found in some enzymes from plant and animal species. The protein is evolutionarily more closely related to this group of enzymes than to histone acetyltransferases. The native protein has a cytosolic cellular location and is present in all three life-cycle stages of the parasite. The recombinant protein was shown to have autoacetylation enzymatic activity.
Materia
Enfermedad de Chagas
Trypanosoma cruzi
Acetiltransferasas
Nivel de accesibilidad
acceso abierto
Condiciones de uso
none
Repositorio
Sistema de Gestión del Conocimiento ANLIS MALBRÁN
Institución
Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
OAI Identificador
oai:sgc.anlis.gob.ar:123456789/1497
Acceder
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network_acronym_str SGCANLIS
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network_name_str Sistema de Gestión del Conocimiento ANLIS MALBRÁN
spelling Characterization of a Trypanosoma cruzi acetyltransferase: cellular location, activity and structureOchaya, StephenRespuela, PatriciaSimonsson, MariaSaraswathi, AbhimanBranche, CaroleLee, JenniferBua, JacquelineNilsson, DanielÅslund, LenaBontempi, EstebanAndersson, BjörnEnfermedad de ChagasTrypanosoma cruziAcetiltransferasasFil: Ochaya, Stephen. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.Fil: Respuela, Patricia. Rudbeck Laboratory. Department of Genetics and Pathology; Suecia.Fil: Simonsson, Maria. Ludwig Institute for Cancer Research; Suecia.Fil: Saraswathi, Abhiman. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.Fil: Branche, Carole. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.Fil: Lee, Jennifer. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.Fil: Bua, Jacqueline. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.Fil: Nilsson, Daniel. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.Fil: Åslund, Lena. Rudbeck Laboratory. Department of Genetics and Pathology; Suecia.Fil: Bontempi, Esteban. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.Fil: Andersson, Björn. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.Trypanosomatids are widespread parasites that cause three major tropical diseases. In trypanosomatids, as in most other organisms, acetylation is a common protein modification that is important in multiple, diverse processes. This paper describes a new member of the Trypanosoma cruzi acetyltransferase family. The gene is single copy and orthologs are also present in the other two sequenced trypanosomatids, Trypanosoma brucei and Leishmania major. This protein (TcAT-1) has the essential motifs present in members of the GCN5-related acetyltransferase (GNAT) family, as well as an additional motif also found in some enzymes from plant and animal species. The protein is evolutionarily more closely related to this group of enzymes than to histone acetyltransferases. The native protein has a cytosolic cellular location and is present in all three life-cycle stages of the parasite. The recombinant protein was shown to have autoacetylation enzymatic activity.2007-04info:ar-repo/semantics/articuloinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdf0166-6851http://sgc.anlis.gob.ar/handle/123456789/149710.1016/j.molbiopara.2006.12.009Molecular and biochemical parasitologynoneinfo:eu-repo/semantics/openAccessengreponame:Sistema de Gestión del Conocimiento ANLIS MALBRÁNinstname:Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"instacron:ANLIS2025-09-04T11:17:12Zoai:sgc.anlis.gob.ar:123456789/1497Institucionalhttp://sgc.anlis.gob.ar/Organismo científico-tecnológicoNo correspondehttp://sgc.anlis.gob.ar/oai/biblioteca@anlis.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:a2025-09-04 11:17:12.437Sistema de Gestión del Conocimiento ANLIS MALBRÁN - Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"false
dc.title.none.fl_str_mv Characterization of a Trypanosoma cruzi acetyltransferase: cellular location, activity and structure
title Characterization of a Trypanosoma cruzi acetyltransferase: cellular location, activity and structure
spellingShingle Characterization of a Trypanosoma cruzi acetyltransferase: cellular location, activity and structure
Ochaya, Stephen
Enfermedad de Chagas
Trypanosoma cruzi
Acetiltransferasas
title_short Characterization of a Trypanosoma cruzi acetyltransferase: cellular location, activity and structure
title_full Characterization of a Trypanosoma cruzi acetyltransferase: cellular location, activity and structure
title_fullStr Characterization of a Trypanosoma cruzi acetyltransferase: cellular location, activity and structure
title_full_unstemmed Characterization of a Trypanosoma cruzi acetyltransferase: cellular location, activity and structure
title_sort Characterization of a Trypanosoma cruzi acetyltransferase: cellular location, activity and structure
dc.creator.none.fl_str_mv Ochaya, Stephen
Respuela, Patricia
Simonsson, Maria
Saraswathi, Abhiman
Branche, Carole
Lee, Jennifer
Bua, Jacqueline
Nilsson, Daniel
Åslund, Lena
Bontempi, Esteban
Andersson, Björn
author Ochaya, Stephen
author_facet Ochaya, Stephen
Respuela, Patricia
Simonsson, Maria
Saraswathi, Abhiman
Branche, Carole
Lee, Jennifer
Bua, Jacqueline
Nilsson, Daniel
Åslund, Lena
Bontempi, Esteban
Andersson, Björn
author_role author
author2 Respuela, Patricia
Simonsson, Maria
Saraswathi, Abhiman
Branche, Carole
Lee, Jennifer
Bua, Jacqueline
Nilsson, Daniel
Åslund, Lena
Bontempi, Esteban
Andersson, Björn
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Enfermedad de Chagas
Trypanosoma cruzi
Acetiltransferasas
topic Enfermedad de Chagas
Trypanosoma cruzi
Acetiltransferasas
dc.description.none.fl_txt_mv Fil: Ochaya, Stephen. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
Fil: Respuela, Patricia. Rudbeck Laboratory. Department of Genetics and Pathology; Suecia.
Fil: Simonsson, Maria. Ludwig Institute for Cancer Research; Suecia.
Fil: Saraswathi, Abhiman. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
Fil: Branche, Carole. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
Fil: Lee, Jennifer. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
Fil: Bua, Jacqueline. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
Fil: Nilsson, Daniel. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
Fil: Åslund, Lena. Rudbeck Laboratory. Department of Genetics and Pathology; Suecia.
Fil: Bontempi, Esteban. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.
Fil: Andersson, Björn. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
Trypanosomatids are widespread parasites that cause three major tropical diseases. In trypanosomatids, as in most other organisms, acetylation is a common protein modification that is important in multiple, diverse processes. This paper describes a new member of the Trypanosoma cruzi acetyltransferase family. The gene is single copy and orthologs are also present in the other two sequenced trypanosomatids, Trypanosoma brucei and Leishmania major. This protein (TcAT-1) has the essential motifs present in members of the GCN5-related acetyltransferase (GNAT) family, as well as an additional motif also found in some enzymes from plant and animal species. The protein is evolutionarily more closely related to this group of enzymes than to histone acetyltransferases. The native protein has a cytosolic cellular location and is present in all three life-cycle stages of the parasite. The recombinant protein was shown to have autoacetylation enzymatic activity.
description Fil: Ochaya, Stephen. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.
publishDate 2007
dc.date.none.fl_str_mv 2007-04
dc.type.none.fl_str_mv info:ar-repo/semantics/articulo
info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv 0166-6851
http://sgc.anlis.gob.ar/handle/123456789/1497
10.1016/j.molbiopara.2006.12.009
identifier_str_mv 0166-6851
10.1016/j.molbiopara.2006.12.009
url http://sgc.anlis.gob.ar/handle/123456789/1497
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Molecular and biochemical parasitology
dc.rights.none.fl_str_mv none
info:eu-repo/semantics/openAccess
rights_invalid_str_mv none
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Sistema de Gestión del Conocimiento ANLIS MALBRÁN
instname:Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
instacron:ANLIS
reponame_str Sistema de Gestión del Conocimiento ANLIS MALBRÁN
collection Sistema de Gestión del Conocimiento ANLIS MALBRÁN
instname_str Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
instacron_str ANLIS
institution ANLIS
repository.name.fl_str_mv Sistema de Gestión del Conocimiento ANLIS MALBRÁN - Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
repository.mail.fl_str_mv biblioteca@anlis.gov.ar
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