All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae

Autores
Nasab, Farnoush Parsaie; Schulz, Benjamin L.; Gamarro, Francisco; Parodi, Armando Jose A.; Aebi, Markus
Año de publicación
2008
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The transfer of lipid-linked oligosaccharide to asparagine residues of polypeptide chains is catalyzed by oligosaccharyltransferase (OTase). In most eukaryotes, OTase is a hetero-oligomeric complex composed of eight different proteins, in which the STT3 component is believed to be the catalytic subunit. In the parasitic protozoa Leishmania major, four STT3 paralogues, but no homologues to the other OTase components seem to be encoded in the genome. We expressed each of the four L. major STT3 proteins individually in Saccharomyces cerevisiae and found that three of them, LmSTT3A, LmSTT3B, and LmSTT3D, were able to complement a deletion of the yeast STT3 locus. Furthermore, LmSTT3D expression suppressed the lethal phenotype of single and double deletions in genes encoding other essential OTase subunits. LmSTT3 proteins did not incorporate into the yeast OTase complex but formed a homodimeric enzyme, capable of replacing the endogenous, multimeric enzyme of the yeast cell. Therefore, these protozoan OTases resemble the prokaryotic enzymes with respect to their architecture, but they used substrates typical for eukaryotic cells: N-X-S/T sequons in proteins and dolicholpyrophosphate-linked high mannose oligosaccharides.
Fil: Nasab, Farnoush Parsaie. Swiss Federal Institute Of Technology Zurich; Suiza
Fil: Schulz, Benjamin L.. Swiss Federal Institute Of Technology Zurich; Suiza
Fil: Gamarro, Francisco. Consejo Superior de Investigaciones Cientificas; España
Fil: Parodi, Armando Jose 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
Fil: Aebi, Markus. Swiss Federal Institute Of Technology Zurich; Suiza
Materia
OLIGOSACCHARYLTRANSFERASE
TRYPANOSOMATIDS
LEISHMANIA
Stt3
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:11336/21122

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network_name_str CONICET Digital (CONICET)
spelling All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiaeNasab, Farnoush ParsaieSchulz, Benjamin L.Gamarro, FranciscoParodi, Armando Jose A.Aebi, MarkusOLIGOSACCHARYLTRANSFERASETRYPANOSOMATIDSLEISHMANIAStt3https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The transfer of lipid-linked oligosaccharide to asparagine residues of polypeptide chains is catalyzed by oligosaccharyltransferase (OTase). In most eukaryotes, OTase is a hetero-oligomeric complex composed of eight different proteins, in which the STT3 component is believed to be the catalytic subunit. In the parasitic protozoa Leishmania major, four STT3 paralogues, but no homologues to the other OTase components seem to be encoded in the genome. We expressed each of the four L. major STT3 proteins individually in Saccharomyces cerevisiae and found that three of them, LmSTT3A, LmSTT3B, and LmSTT3D, were able to complement a deletion of the yeast STT3 locus. Furthermore, LmSTT3D expression suppressed the lethal phenotype of single and double deletions in genes encoding other essential OTase subunits. LmSTT3 proteins did not incorporate into the yeast OTase complex but formed a homodimeric enzyme, capable of replacing the endogenous, multimeric enzyme of the yeast cell. Therefore, these protozoan OTases resemble the prokaryotic enzymes with respect to their architecture, but they used substrates typical for eukaryotic cells: N-X-S/T sequons in proteins and dolicholpyrophosphate-linked high mannose oligosaccharides.Fil: Nasab, Farnoush Parsaie. Swiss Federal Institute Of Technology Zurich; SuizaFil: Schulz, Benjamin L.. Swiss Federal Institute Of Technology Zurich; SuizaFil: Gamarro, Francisco. Consejo Superior de Investigaciones Cientificas; EspañaFil: Parodi, Armando Jose 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; ArgentinaFil: Aebi, Markus. Swiss Federal Institute Of Technology Zurich; SuizaAmerican Society for Cell Biology2008-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/21122Nasab, Farnoush Parsaie; Schulz, Benjamin L.; Gamarro, Francisco; Parodi, Armando Jose A.; Aebi, Markus; All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae; American Society for Cell Biology; Molecular Biology Of The Cell; 19; 9; 7-2008; 3758-37681059-15241939-4586CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.molbiolcell.org/content/19/9/3758.longinfo:eu-repo/semantics/altIdentifier/doi/10.1091/mbc.E08-05-0467info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:42:43Zoai:ri.conicet.gov.ar:11336/21122instacron: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:34982025-10-15 15:42:43.789CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae
title All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae
spellingShingle All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae
Nasab, Farnoush Parsaie
OLIGOSACCHARYLTRANSFERASE
TRYPANOSOMATIDS
LEISHMANIA
Stt3
title_short All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae
title_full All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae
title_fullStr All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae
title_full_unstemmed All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae
title_sort All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae
dc.creator.none.fl_str_mv Nasab, Farnoush Parsaie
Schulz, Benjamin L.
Gamarro, Francisco
Parodi, Armando Jose A.
Aebi, Markus
author Nasab, Farnoush Parsaie
author_facet Nasab, Farnoush Parsaie
Schulz, Benjamin L.
Gamarro, Francisco
Parodi, Armando Jose A.
Aebi, Markus
author_role author
author2 Schulz, Benjamin L.
Gamarro, Francisco
Parodi, Armando Jose A.
Aebi, Markus
author2_role author
author
author
author
dc.subject.none.fl_str_mv OLIGOSACCHARYLTRANSFERASE
TRYPANOSOMATIDS
LEISHMANIA
Stt3
topic OLIGOSACCHARYLTRANSFERASE
TRYPANOSOMATIDS
LEISHMANIA
Stt3
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The transfer of lipid-linked oligosaccharide to asparagine residues of polypeptide chains is catalyzed by oligosaccharyltransferase (OTase). In most eukaryotes, OTase is a hetero-oligomeric complex composed of eight different proteins, in which the STT3 component is believed to be the catalytic subunit. In the parasitic protozoa Leishmania major, four STT3 paralogues, but no homologues to the other OTase components seem to be encoded in the genome. We expressed each of the four L. major STT3 proteins individually in Saccharomyces cerevisiae and found that three of them, LmSTT3A, LmSTT3B, and LmSTT3D, were able to complement a deletion of the yeast STT3 locus. Furthermore, LmSTT3D expression suppressed the lethal phenotype of single and double deletions in genes encoding other essential OTase subunits. LmSTT3 proteins did not incorporate into the yeast OTase complex but formed a homodimeric enzyme, capable of replacing the endogenous, multimeric enzyme of the yeast cell. Therefore, these protozoan OTases resemble the prokaryotic enzymes with respect to their architecture, but they used substrates typical for eukaryotic cells: N-X-S/T sequons in proteins and dolicholpyrophosphate-linked high mannose oligosaccharides.
Fil: Nasab, Farnoush Parsaie. Swiss Federal Institute Of Technology Zurich; Suiza
Fil: Schulz, Benjamin L.. Swiss Federal Institute Of Technology Zurich; Suiza
Fil: Gamarro, Francisco. Consejo Superior de Investigaciones Cientificas; España
Fil: Parodi, Armando Jose 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
Fil: Aebi, Markus. Swiss Federal Institute Of Technology Zurich; Suiza
description The transfer of lipid-linked oligosaccharide to asparagine residues of polypeptide chains is catalyzed by oligosaccharyltransferase (OTase). In most eukaryotes, OTase is a hetero-oligomeric complex composed of eight different proteins, in which the STT3 component is believed to be the catalytic subunit. In the parasitic protozoa Leishmania major, four STT3 paralogues, but no homologues to the other OTase components seem to be encoded in the genome. We expressed each of the four L. major STT3 proteins individually in Saccharomyces cerevisiae and found that three of them, LmSTT3A, LmSTT3B, and LmSTT3D, were able to complement a deletion of the yeast STT3 locus. Furthermore, LmSTT3D expression suppressed the lethal phenotype of single and double deletions in genes encoding other essential OTase subunits. LmSTT3 proteins did not incorporate into the yeast OTase complex but formed a homodimeric enzyme, capable of replacing the endogenous, multimeric enzyme of the yeast cell. Therefore, these protozoan OTases resemble the prokaryotic enzymes with respect to their architecture, but they used substrates typical for eukaryotic cells: N-X-S/T sequons in proteins and dolicholpyrophosphate-linked high mannose oligosaccharides.
publishDate 2008
dc.date.none.fl_str_mv 2008-07
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/11336/21122
Nasab, Farnoush Parsaie; Schulz, Benjamin L.; Gamarro, Francisco; Parodi, Armando Jose A.; Aebi, Markus; All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae; American Society for Cell Biology; Molecular Biology Of The Cell; 19; 9; 7-2008; 3758-3768
1059-1524
1939-4586
CONICET Digital
CONICET
url http://hdl.handle.net/11336/21122
identifier_str_mv Nasab, Farnoush Parsaie; Schulz, Benjamin L.; Gamarro, Francisco; Parodi, Armando Jose A.; Aebi, Markus; All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae; American Society for Cell Biology; Molecular Biology Of The Cell; 19; 9; 7-2008; 3758-3768
1059-1524
1939-4586
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.molbiolcell.org/content/19/9/3758.long
info:eu-repo/semantics/altIdentifier/doi/10.1091/mbc.E08-05-0467
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
dc.publisher.none.fl_str_mv American Society for Cell Biology
publisher.none.fl_str_mv American Society for Cell Biology
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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