Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction

Detalhes bibliográficos
Autor(a) principal: Bule, Pedro
Data de Publicação: 2018
Outros Autores: Pires, Virgínia M. R., Alves, Victor D., Carvalho, Ana Luísa, Prates, José A. M., Ferreira, Luís M. A., Smith, Steven P., Gilbert, Harry J., Noach, Ilit, Bayer, Edward A., Najmudin, Shabir, Fontes, Carlos M.G.A.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://doi.org/10.1038/s41598-018-25171-8
Resumo: The authors acknowledge financial support from Fundacao para a Ciencia e a Tecnologia (Lisbon, Portugal) through grants PTDC/BIA-MIC/5947/2014, RECI/BBB-BEP/0124/2012 while PB and VMRP were supported by the individual fellowships SFRH/BD/86821/2012 and IF/01621/2013, respectively. The authors also acknowledge Professor Maria Joao Romao for access to the crystallization facilities of the Protein Crystallography Group in the Faculty of Science and Technology, Universidade NOVA de Lisboa, as well as the Soleil synchrotron, L'Orme des Merisiers, Saint-Aubin, France, (beamline PROXIMA-1) for access and technical support during data collection, and the European Community's Seventh Framework Programme (FP7/2007-2013) under BioStruct-X (grant agreement No. 283570, proposal number: Biostruct-X_4399) for funding. The Unidade de Ciencias Biomoleculares Aplicadas (UCIBIO- REQUIMTE) is financed by national funds from Fundacao para a Ciencia e Tecnologia/Ministerio da Educacao e Ciencia (FCT/ME) (UID/Multi/04378/2013) and co-financed by the European Regional Development Fund under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728).
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spelling Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interactionClostridium thermocellumCellulosomesConsolidated bioprocessingGeneralThe authors acknowledge financial support from Fundacao para a Ciencia e a Tecnologia (Lisbon, Portugal) through grants PTDC/BIA-MIC/5947/2014, RECI/BBB-BEP/0124/2012 while PB and VMRP were supported by the individual fellowships SFRH/BD/86821/2012 and IF/01621/2013, respectively. The authors also acknowledge Professor Maria Joao Romao for access to the crystallization facilities of the Protein Crystallography Group in the Faculty of Science and Technology, Universidade NOVA de Lisboa, as well as the Soleil synchrotron, L'Orme des Merisiers, Saint-Aubin, France, (beamline PROXIMA-1) for access and technical support during data collection, and the European Community's Seventh Framework Programme (FP7/2007-2013) under BioStruct-X (grant agreement No. 283570, proposal number: Biostruct-X_4399) for funding. The Unidade de Ciencias Biomoleculares Aplicadas (UCIBIO- REQUIMTE) is financed by national funds from Fundacao para a Ciencia e Tecnologia/Ministerio da Educacao e Ciencia (FCT/ME) (UID/Multi/04378/2013) and co-financed by the European Regional Development Fund under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728).Cellulosomes are highly sophisticated molecular nanomachines that participate in the deconstruction of complex polysaccharides, notably cellulose and hemicellulose. Cellulosomal assembly is orchestrated by the interaction of enzyme-borne dockerin (Doc) modules to tandem cohesin (Coh) modules of a non-catalytic primary scaffoldin. In some cases, as exemplified by the cellulosome of the major cellulolytic ruminal bacterium Ruminococcus flavefaciens, primary scaffoldins bind to adaptor scaffoldins that further interact with the cell surface via anchoring scaffoldins, thereby increasing cellulosome complexity. Here we elucidate the structure of the unique Doc of R. flavefaciens FD-1 primary scaffoldin ScaA, bound to Coh 5 of the adaptor scaffoldin ScaB. The RfCohScaB5-DocScaA complex has an elliptical architecture similar to previously described complexes from a variety of ecological niches. ScaA Doc presents a single-binding mode, analogous to that described for the other two Coh-Doc specificities required for cellulosome assembly in R. flavefaciens. The exclusive reliance on a single-mode of Coh recognition contrasts with the majority of cellulosomes from other bacterial species described to date, where Docs contain two similar Coh-binding interfaces promoting a dual-binding mode. The discrete Coh-Doc interactions observed in ruminal cellulosomes suggest an adaptation to the exquisite properties of the rumen environment.UCIBIO - Applied Molecular Biosciences UnitDQ - Departamento de QuímicaRUNBule, PedroPires, Virgínia M. R.Alves, Victor D.Carvalho, Ana LuísaPrates, José A. M.Ferreira, Luís M. A.Smith, Steven P.Gilbert, Harry J.Noach, IlitBayer, Edward A.Najmudin, ShabirFontes, Carlos M.G.A.2019-01-25T23:40:18Z2018-12-012018-12-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://doi.org/10.1038/s41598-018-25171-8eng2045-2322PURE: 4372685http://www.scopus.com/inward/record.url?scp=85046619629&partnerID=8YFLogxKhttps://doi.org/10.1038/s41598-018-25171-8info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T04:28:18Zoai:run.unl.pt:10362/58650Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:33:18.050480Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction
title Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction
spellingShingle Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction
Bule, Pedro
Clostridium thermocellum
Cellulosomes
Consolidated bioprocessing
General
title_short Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction
title_full Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction
title_fullStr Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction
title_full_unstemmed Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction
title_sort Higher order scaffoldin assembly in Ruminococcus flavefaciens cellulosome is coordinated by a discrete cohesin-dockerin interaction
author Bule, Pedro
author_facet Bule, Pedro
Pires, Virgínia M. R.
Alves, Victor D.
Carvalho, Ana Luísa
Prates, José A. M.
Ferreira, Luís M. A.
Smith, Steven P.
Gilbert, Harry J.
Noach, Ilit
Bayer, Edward A.
Najmudin, Shabir
Fontes, Carlos M.G.A.
author_role author
author2 Pires, Virgínia M. R.
Alves, Victor D.
Carvalho, Ana Luísa
Prates, José A. M.
Ferreira, Luís M. A.
Smith, Steven P.
Gilbert, Harry J.
Noach, Ilit
Bayer, Edward A.
Najmudin, Shabir
Fontes, Carlos M.G.A.
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv UCIBIO - Applied Molecular Biosciences Unit
DQ - Departamento de Química
RUN
dc.contributor.author.fl_str_mv Bule, Pedro
Pires, Virgínia M. R.
Alves, Victor D.
Carvalho, Ana Luísa
Prates, José A. M.
Ferreira, Luís M. A.
Smith, Steven P.
Gilbert, Harry J.
Noach, Ilit
Bayer, Edward A.
Najmudin, Shabir
Fontes, Carlos M.G.A.
dc.subject.por.fl_str_mv Clostridium thermocellum
Cellulosomes
Consolidated bioprocessing
General
topic Clostridium thermocellum
Cellulosomes
Consolidated bioprocessing
General
description The authors acknowledge financial support from Fundacao para a Ciencia e a Tecnologia (Lisbon, Portugal) through grants PTDC/BIA-MIC/5947/2014, RECI/BBB-BEP/0124/2012 while PB and VMRP were supported by the individual fellowships SFRH/BD/86821/2012 and IF/01621/2013, respectively. The authors also acknowledge Professor Maria Joao Romao for access to the crystallization facilities of the Protein Crystallography Group in the Faculty of Science and Technology, Universidade NOVA de Lisboa, as well as the Soleil synchrotron, L'Orme des Merisiers, Saint-Aubin, France, (beamline PROXIMA-1) for access and technical support during data collection, and the European Community's Seventh Framework Programme (FP7/2007-2013) under BioStruct-X (grant agreement No. 283570, proposal number: Biostruct-X_4399) for funding. The Unidade de Ciencias Biomoleculares Aplicadas (UCIBIO- REQUIMTE) is financed by national funds from Fundacao para a Ciencia e Tecnologia/Ministerio da Educacao e Ciencia (FCT/ME) (UID/Multi/04378/2013) and co-financed by the European Regional Development Fund under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728).
publishDate 2018
dc.date.none.fl_str_mv 2018-12-01
2018-12-01T00:00:00Z
2019-01-25T23:40:18Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://doi.org/10.1038/s41598-018-25171-8
url https://doi.org/10.1038/s41598-018-25171-8
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2045-2322
PURE: 4372685
http://www.scopus.com/inward/record.url?scp=85046619629&partnerID=8YFLogxK
https://doi.org/10.1038/s41598-018-25171-8
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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