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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/21122
Ver los metadatos del registro completo
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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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1846083535041986560 |
score |
13.22299 |