Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit

Autores
Castro, Olga Alejandra; Movsichoff, Federico; Parodi, Armando José A.
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Most eukaryotic cells show a strong preference for the transfer in vivo and in vitro of the largest dolichol-P-P-linked glycan (Glc3Man 9GlcNAc2) to protein chains over that of biosynthetic intermediates that lack the full complement of glucose units. The oligosaccharyltransferase (OST) is a multimeric complex containing eight different proteins, one of which (Stt3p) is the catalytic subunit. Trypanosomatid protozoa lack an OST complex and express only this last protein. Contrary to the OST complex from most eukaryotic cells, the Stt3p subunit of these parasites transfers in cell-free assays glycans with Man 7-9GlcNAc2 and Glc1-3Man9GlcNAc 2 compositions at the same rate. We have replaced Saccharomyces cerevisiae Stt3p by the Trypanosoma cruzi homologue and found that the complex that is formed preferentially transfers the complete glycan both in vivo and in vitro. Thus, preference for Glc3Man9GlcNAc2 is a feature that is determined by the complex and not by the catalytic subunit.
Fil: Castro, Olga Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Movsichoff, Federico. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Parodi, Armando José A.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Materia
N-GLYCOSYLATION
SACCHAROMYCES CEREVISIAE
TRYPANOSOMA CRUZI
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/39504
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunitCastro, Olga AlejandraMovsichoff, FedericoParodi, Armando José A.N-GLYCOSYLATIONSACCHAROMYCES CEREVISIAETRYPANOSOMA CRUZIhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Most eukaryotic cells show a strong preference for the transfer in vivo and in vitro of the largest dolichol-P-P-linked glycan (Glc3Man 9GlcNAc2) to protein chains over that of biosynthetic intermediates that lack the full complement of glucose units. The oligosaccharyltransferase (OST) is a multimeric complex containing eight different proteins, one of which (Stt3p) is the catalytic subunit. Trypanosomatid protozoa lack an OST complex and express only this last protein. Contrary to the OST complex from most eukaryotic cells, the Stt3p subunit of these parasites transfers in cell-free assays glycans with Man 7-9GlcNAc2 and Glc1-3Man9GlcNAc 2 compositions at the same rate. We have replaced Saccharomyces cerevisiae Stt3p by the Trypanosoma cruzi homologue and found that the complex that is formed preferentially transfers the complete glycan both in vivo and in vitro. Thus, preference for Glc3Man9GlcNAc2 is a feature that is determined by the complex and not by the catalytic subunit.Fil: Castro, Olga Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Movsichoff, Federico. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Parodi, Armando José A.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaNational Academy of Sciences2006-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/39504Castro, Olga Alejandra; Movsichoff, Federico; Parodi, Armando José A.; Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 103; 40; 10-2006; 14756-147600027-84241091-6490CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/103/40/14756.longinfo:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.0607086103info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:57:35Zoai:ri.conicet.gov.ar:11336/39504instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:57:35.904CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit
title Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit
spellingShingle Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit
Castro, Olga Alejandra
N-GLYCOSYLATION
SACCHAROMYCES CEREVISIAE
TRYPANOSOMA CRUZI
title_short Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit
title_full Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit
title_fullStr Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit
title_full_unstemmed Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit
title_sort Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit
dc.creator.none.fl_str_mv Castro, Olga Alejandra
Movsichoff, Federico
Parodi, Armando José A.
author Castro, Olga Alejandra
author_facet Castro, Olga Alejandra
Movsichoff, Federico
Parodi, Armando José A.
author_role author
author2 Movsichoff, Federico
Parodi, Armando José A.
author2_role author
author
dc.subject.none.fl_str_mv N-GLYCOSYLATION
SACCHAROMYCES CEREVISIAE
TRYPANOSOMA CRUZI
topic N-GLYCOSYLATION
SACCHAROMYCES CEREVISIAE
TRYPANOSOMA CRUZI
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Most eukaryotic cells show a strong preference for the transfer in vivo and in vitro of the largest dolichol-P-P-linked glycan (Glc3Man 9GlcNAc2) to protein chains over that of biosynthetic intermediates that lack the full complement of glucose units. The oligosaccharyltransferase (OST) is a multimeric complex containing eight different proteins, one of which (Stt3p) is the catalytic subunit. Trypanosomatid protozoa lack an OST complex and express only this last protein. Contrary to the OST complex from most eukaryotic cells, the Stt3p subunit of these parasites transfers in cell-free assays glycans with Man 7-9GlcNAc2 and Glc1-3Man9GlcNAc 2 compositions at the same rate. We have replaced Saccharomyces cerevisiae Stt3p by the Trypanosoma cruzi homologue and found that the complex that is formed preferentially transfers the complete glycan both in vivo and in vitro. Thus, preference for Glc3Man9GlcNAc2 is a feature that is determined by the complex and not by the catalytic subunit.
Fil: Castro, Olga Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Movsichoff, Federico. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Parodi, Armando José A.. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
description Most eukaryotic cells show a strong preference for the transfer in vivo and in vitro of the largest dolichol-P-P-linked glycan (Glc3Man 9GlcNAc2) to protein chains over that of biosynthetic intermediates that lack the full complement of glucose units. The oligosaccharyltransferase (OST) is a multimeric complex containing eight different proteins, one of which (Stt3p) is the catalytic subunit. Trypanosomatid protozoa lack an OST complex and express only this last protein. Contrary to the OST complex from most eukaryotic cells, the Stt3p subunit of these parasites transfers in cell-free assays glycans with Man 7-9GlcNAc2 and Glc1-3Man9GlcNAc 2 compositions at the same rate. We have replaced Saccharomyces cerevisiae Stt3p by the Trypanosoma cruzi homologue and found that the complex that is formed preferentially transfers the complete glycan both in vivo and in vitro. Thus, preference for Glc3Man9GlcNAc2 is a feature that is determined by the complex and not by the catalytic subunit.
publishDate 2006
dc.date.none.fl_str_mv 2006-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/39504
Castro, Olga Alejandra; Movsichoff, Federico; Parodi, Armando José A.; Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 103; 40; 10-2006; 14756-14760
0027-8424
1091-6490
CONICET Digital
CONICET
url http://hdl.handle.net/11336/39504
identifier_str_mv Castro, Olga Alejandra; Movsichoff, Federico; Parodi, Armando José A.; Preferential transfer of the complete glycan is determined by the oligosaccharyltransferase complex and not by the catalytic subunit; National Academy of Sciences; Proceedings of the National Academy of Sciences of The United States of America; 103; 40; 10-2006; 14756-14760
0027-8424
1091-6490
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/103/40/14756.long
info:eu-repo/semantics/altIdentifier/doi/10.1073/pnas.0607086103
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv National Academy of Sciences
publisher.none.fl_str_mv National Academy of Sciences
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.069144

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