Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilum

Autores
Premageetha, Gowtham Thambra Rajan; Dhanabalan, KanagaVijayan; Bose, Sucharita; Manjunath, Lavanyaa; Joseph, Deepthi; Paz, Aviv; Grandfield, Samuel; Nayak, Vinod; Bredeston, Luis María; Abramson, Jeff; Ramaswamy, Subramanian
Año de publicación
2023
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Nucleotide Sugar Transporters (NSTs) belong to the SLC35 family (human solute carrier) of membrane transport proteins and are crucial components of the glycosylation machinery. NSTs are localized in the ER and Golgi apparatus membranes, where they accumulate nucleotide sugars from the cytosol for subsequent polysaccharide biosynthesis. Loss of NST function impacts the glycosylation of cell surface molecules. Mutations in NSTs cause several developmental disorders, immune disorders, and increased susceptibility to infection. Atomic resolution structures of three NSTs have provided a blueprint for a detailed molecular interpretation of their biochemical properties. In this work, we have identified, cloned, and expressed 18 members of the SLC35 family from various eukaryotic organisms in Saccharomyces cerevisiae. Out of 18 clones, we determined Vrg4 from Chaetomium thermophilum (CtVrg4) is a GDP-mannose transporter with an enhanced melting point temperature (Tm) of 56.9̊C, which increases with the addition of substrates, GMP and GDP-mannose. In addition, we report—for the first time—that the CtVrg4 shows an affinity to bind to phosphatidylinositol lipids.
Fil: Premageetha, Gowtham Thambra Rajan. Purdue University; Estados Unidos. Manipal Academy Of Higher Education; India. Institute For Stem Cell Science And Regenerative Medicine; India
Fil: Dhanabalan, KanagaVijayan. Institute For Stem Cell Science And Regenerative Medicine; India. Purdue University; Estados Unidos
Fil: Bose, Sucharita. Institute For Stem Cell Science And Regenerative Medicine; India
Fil: Manjunath, Lavanyaa. Institute For Stem Cell Science And Regenerative Medicine; India
Fil: Joseph, Deepthi. Institute For Stem Cell Science And Regenerative Medicine; India
Fil: Paz, Aviv. University of California at Los Angeles. School of Medicine; Estados Unidos
Fil: Grandfield, Samuel. University of California at Los Angeles. School of Medicine; Estados Unidos
Fil: Nayak, Vinod. Institute For Stem Cell Science And Regenerative Medicine; India
Fil: Bredeston, Luis María. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Abramson, Jeff. University of California at Los Angeles. School of Medicine; Estados Unidos
Fil: Ramaswamy, Subramanian. Purdue University; Estados Unidos. Institute For Stem Cell Science And Regenerative Medicine; India
Materia
Nucleotide Sugar Transporters
Golgi
GDP-mannose
Chaetomium thermophilum
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/227935
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/227935
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilumPremageetha, Gowtham Thambra RajanDhanabalan, KanagaVijayanBose, SucharitaManjunath, LavanyaaJoseph, DeepthiPaz, AvivGrandfield, SamuelNayak, VinodBredeston, Luis MaríaAbramson, JeffRamaswamy, SubramanianNucleotide Sugar TransportersGolgiGDP-mannoseChaetomium thermophilumhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Nucleotide Sugar Transporters (NSTs) belong to the SLC35 family (human solute carrier) of membrane transport proteins and are crucial components of the glycosylation machinery. NSTs are localized in the ER and Golgi apparatus membranes, where they accumulate nucleotide sugars from the cytosol for subsequent polysaccharide biosynthesis. Loss of NST function impacts the glycosylation of cell surface molecules. Mutations in NSTs cause several developmental disorders, immune disorders, and increased susceptibility to infection. Atomic resolution structures of three NSTs have provided a blueprint for a detailed molecular interpretation of their biochemical properties. In this work, we have identified, cloned, and expressed 18 members of the SLC35 family from various eukaryotic organisms in Saccharomyces cerevisiae. Out of 18 clones, we determined Vrg4 from Chaetomium thermophilum (CtVrg4) is a GDP-mannose transporter with an enhanced melting point temperature (Tm) of 56.9̊C, which increases with the addition of substrates, GMP and GDP-mannose. In addition, we report—for the first time—that the CtVrg4 shows an affinity to bind to phosphatidylinositol lipids.Fil: Premageetha, Gowtham Thambra Rajan. Purdue University; Estados Unidos. Manipal Academy Of Higher Education; India. Institute For Stem Cell Science And Regenerative Medicine; IndiaFil: Dhanabalan, KanagaVijayan. Institute For Stem Cell Science And Regenerative Medicine; India. Purdue University; Estados UnidosFil: Bose, Sucharita. Institute For Stem Cell Science And Regenerative Medicine; IndiaFil: Manjunath, Lavanyaa. Institute For Stem Cell Science And Regenerative Medicine; IndiaFil: Joseph, Deepthi. Institute For Stem Cell Science And Regenerative Medicine; IndiaFil: Paz, Aviv. University of California at Los Angeles. School of Medicine; Estados UnidosFil: Grandfield, Samuel. University of California at Los Angeles. School of Medicine; Estados UnidosFil: Nayak, Vinod. Institute For Stem Cell Science And Regenerative Medicine; IndiaFil: Bredeston, Luis María. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; ArgentinaFil: Abramson, Jeff. University of California at Los Angeles. School of Medicine; Estados UnidosFil: Ramaswamy, Subramanian. Purdue University; Estados Unidos. Institute For Stem Cell Science And Regenerative Medicine; IndiaPublic Library of Science2023-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/227935Premageetha, Gowtham Thambra Rajan; Dhanabalan, KanagaVijayan; Bose, Sucharita; Manjunath, Lavanyaa; Joseph, Deepthi; et al.; Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilum; Public Library of Science; Plos One; 18; 5-2023; 1-151932-6203CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0280975info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0280975info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:37:56Zoai:ri.conicet.gov.ar:11336/227935instacron: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:34982025-10-22 11:37:56.925CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilum
title Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilum
spellingShingle Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilum
Premageetha, Gowtham Thambra Rajan
Nucleotide Sugar Transporters
Golgi
GDP-mannose
Chaetomium thermophilum
title_short Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilum
title_full Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilum
title_fullStr Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilum
title_full_unstemmed Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilum
title_sort Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilum
dc.creator.none.fl_str_mv Premageetha, Gowtham Thambra Rajan
Dhanabalan, KanagaVijayan
Bose, Sucharita
Manjunath, Lavanyaa
Joseph, Deepthi
Paz, Aviv
Grandfield, Samuel
Nayak, Vinod
Bredeston, Luis María
Abramson, Jeff
Ramaswamy, Subramanian
author Premageetha, Gowtham Thambra Rajan
author_facet Premageetha, Gowtham Thambra Rajan
Dhanabalan, KanagaVijayan
Bose, Sucharita
Manjunath, Lavanyaa
Joseph, Deepthi
Paz, Aviv
Grandfield, Samuel
Nayak, Vinod
Bredeston, Luis María
Abramson, Jeff
Ramaswamy, Subramanian
author_role author
author2 Dhanabalan, KanagaVijayan
Bose, Sucharita
Manjunath, Lavanyaa
Joseph, Deepthi
Paz, Aviv
Grandfield, Samuel
Nayak, Vinod
Bredeston, Luis María
Abramson, Jeff
Ramaswamy, Subramanian
author2_role author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Nucleotide Sugar Transporters
Golgi
GDP-mannose
Chaetomium thermophilum
topic Nucleotide Sugar Transporters
Golgi
GDP-mannose
Chaetomium thermophilum
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Nucleotide Sugar Transporters (NSTs) belong to the SLC35 family (human solute carrier) of membrane transport proteins and are crucial components of the glycosylation machinery. NSTs are localized in the ER and Golgi apparatus membranes, where they accumulate nucleotide sugars from the cytosol for subsequent polysaccharide biosynthesis. Loss of NST function impacts the glycosylation of cell surface molecules. Mutations in NSTs cause several developmental disorders, immune disorders, and increased susceptibility to infection. Atomic resolution structures of three NSTs have provided a blueprint for a detailed molecular interpretation of their biochemical properties. In this work, we have identified, cloned, and expressed 18 members of the SLC35 family from various eukaryotic organisms in Saccharomyces cerevisiae. Out of 18 clones, we determined Vrg4 from Chaetomium thermophilum (CtVrg4) is a GDP-mannose transporter with an enhanced melting point temperature (Tm) of 56.9̊C, which increases with the addition of substrates, GMP and GDP-mannose. In addition, we report—for the first time—that the CtVrg4 shows an affinity to bind to phosphatidylinositol lipids.
Fil: Premageetha, Gowtham Thambra Rajan. Purdue University; Estados Unidos. Manipal Academy Of Higher Education; India. Institute For Stem Cell Science And Regenerative Medicine; India
Fil: Dhanabalan, KanagaVijayan. Institute For Stem Cell Science And Regenerative Medicine; India. Purdue University; Estados Unidos
Fil: Bose, Sucharita. Institute For Stem Cell Science And Regenerative Medicine; India
Fil: Manjunath, Lavanyaa. Institute For Stem Cell Science And Regenerative Medicine; India
Fil: Joseph, Deepthi. Institute For Stem Cell Science And Regenerative Medicine; India
Fil: Paz, Aviv. University of California at Los Angeles. School of Medicine; Estados Unidos
Fil: Grandfield, Samuel. University of California at Los Angeles. School of Medicine; Estados Unidos
Fil: Nayak, Vinod. Institute For Stem Cell Science And Regenerative Medicine; India
Fil: Bredeston, Luis María. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
Fil: Abramson, Jeff. University of California at Los Angeles. School of Medicine; Estados Unidos
Fil: Ramaswamy, Subramanian. Purdue University; Estados Unidos. Institute For Stem Cell Science And Regenerative Medicine; India
description Nucleotide Sugar Transporters (NSTs) belong to the SLC35 family (human solute carrier) of membrane transport proteins and are crucial components of the glycosylation machinery. NSTs are localized in the ER and Golgi apparatus membranes, where they accumulate nucleotide sugars from the cytosol for subsequent polysaccharide biosynthesis. Loss of NST function impacts the glycosylation of cell surface molecules. Mutations in NSTs cause several developmental disorders, immune disorders, and increased susceptibility to infection. Atomic resolution structures of three NSTs have provided a blueprint for a detailed molecular interpretation of their biochemical properties. In this work, we have identified, cloned, and expressed 18 members of the SLC35 family from various eukaryotic organisms in Saccharomyces cerevisiae. Out of 18 clones, we determined Vrg4 from Chaetomium thermophilum (CtVrg4) is a GDP-mannose transporter with an enhanced melting point temperature (Tm) of 56.9̊C, which increases with the addition of substrates, GMP and GDP-mannose. In addition, we report—for the first time—that the CtVrg4 shows an affinity to bind to phosphatidylinositol lipids.
publishDate 2023
dc.date.none.fl_str_mv 2023-05
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/11336/227935
Premageetha, Gowtham Thambra Rajan; Dhanabalan, KanagaVijayan; Bose, Sucharita; Manjunath, Lavanyaa; Joseph, Deepthi; et al.; Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilum; Public Library of Science; Plos One; 18; 5-2023; 1-15
1932-6203
CONICET Digital
CONICET
url http://hdl.handle.net/11336/227935
identifier_str_mv Premageetha, Gowtham Thambra Rajan; Dhanabalan, KanagaVijayan; Bose, Sucharita; Manjunath, Lavanyaa; Joseph, Deepthi; et al.; Biochemical characterization of a GDP-mannose transporter from Chaetomium thermophilum; Public Library of Science; Plos One; 18; 5-2023; 1-15
1932-6203
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0280975
info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0280975
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Public Library of Science
publisher.none.fl_str_mv Public Library of Science
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 12.982451

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