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Diverse specificity of cellulosome attachment to the bacterial cell surface

2016-12-07Artigo científico Acesso aberto
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dc.contributor.authorBrás, Joana L. A.
dc.contributor.authorPinheiro, Benedita A.
dc.contributor.authorCameron, Kate
dc.contributor.authorCuskin, Fiona
dc.contributor.authorViegas, Aldino
dc.contributor.authorNajmudin, Shabir
dc.contributor.authorBule, Pedro
dc.contributor.authorPires, Virginia M. R.
dc.contributor.authorRomão, Maria João
dc.contributor.authorBayer, Edward A.
dc.contributor.authorSpencer, Holly L
dc.contributor.authorSmith, Steven P
dc.contributor.authorGilbert, Harry J.
dc.contributor.authorAlves, Victor D
dc.contributor.authorCarvalho, Ana Luísa
dc.contributor.authorFontes, Carlos M. G. A.
dc.contributor.institutionUCIBIO - Applied Molecular Biosciences Unit
dc.contributor.institutionDQ - Departamento de Química
dc.contributor.pblNature Publishing Group
dc.date.accessioned2018-05-14T22:04:35Z
dc.date.available2018-05-14T22:04:35Z
dc.date.issued2016-12-07
dc.descriptionThis work was supported by the EU FP7 programme under the WallTraC project (grant No. 263916) and by projects PTDC/BIA-MIC/5947/2014, RECI/BBB-BEP/0124/2012 and EXPL/BIA-MIC/1176/2012 supported by Fundacao para a Ciencia e Tecnologia (FCT-MCTES). The Research Unit UCIBIO (Unidade de Ciencias Biomoleculares Aplicadas) is financed by national funds from FCT/MCTES EC (UID/Multi/04378/2013) and co-financed by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728). We thank the European Synchrotron Radiation Facility (Grenoble, France), Soleil (Saint-Aubin, France) and Diamond Light Source (Harwell, UK) for 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.
dc.description.abstractDuring the course of evolution, the cellulosome, one of Nature's most intricate multi-enzyme complexes, has been continuously fine-tuned to efficiently deconstruct recalcitrant carbohydrates. To facilitate the uptake of released sugars, anaerobic bacteria use highly ordered protein-protein interactions to recruit these nanomachines to the cell surface. Dockerin modules located within a non-catalytic macromolecular scaffold, whose primary role is to assemble cellulosomal enzymatic subunits, bind cohesin modules of cell envelope proteins, thereby anchoring the cellulosome onto the bacterial cell. Here we have elucidated the unique molecular mechanisms used by anaerobic bacteria for cellulosome cellular attachment. The structure and biochemical analysis of five cohesin-dockerin complexes revealed that cell surface dockerins contain two cohesin-binding interfaces, which can present different or identical specificities. In contrast to the current static model, we propose that dockerins utilize multivalent modes of cohesin recognition to recruit cellulosomes to the cell surface, a mechanism that maximises substrate access while facilitating complex assembly.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent12
dc.format.extent2377127
dc.identifier.doi10.1038/srep38292
dc.identifier.issn2045-2322
dc.identifier.otherPURE: 2517978
dc.identifier.otherPURE UUID: 74845819-6728-4765-8e52-ea72c70e9af4
dc.identifier.otherPubMed: 27924829
dc.identifier.otherPubMedCentral: PMC5141474
dc.identifier.otherScopus: 85002651253
dc.identifier.otherWOS: 000389700700001
dc.identifier.otherORCID: /0000-0002-3004-0543/work/54825306
dc.identifier.otherORCID: /0000-0002-3824-0240/work/54825444
dc.identifier.urihttp://hdl.handle.net/10362/36982
dc.language.isoeng
dc.peerreviewedyes
dc.subjectCOHESIN-DOCKERIN COMPLEX
dc.subjectDUAL BINDING MODE
dc.subjectCLOSTRIDIUM-THERMOCELLUM
dc.subjectCRYSTAL-STRUCTURE
dc.subjectMODULES
dc.subjectDOMAIN
dc.titleDiverse specificity of cellulosome attachment to the bacterial cell surfaceen
dc.typejournal article
degois.publication.titleScientific Reports
degois.publication.volume6
dspace.entity.typePublication
rcaap.rightsopenAccess

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