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dc.contributor.author | Brasch, Melanie | |
dc.contributor.author | Putri, Rindia M. | |
dc.contributor.author | de Ruiter, Mark V. | |
dc.contributor.author | Luque, Daniel | |
dc.contributor.author | Koay, Melissa. S. T. | |
dc.contributor.author | Castón, José R. | |
dc.contributor.author | Cornelissen, Jeroen J. L. M. | |
dc.date.accessioned | 2019-05-30T10:45:30Z | |
dc.date.available | 2019-05-30T10:45:30Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | J. Am. Chem. Soc.2017,139,4,1512-1519 | es_ES |
dc.identifier.issn | 0002-7863 | es_ES |
dc.identifier.uri | http://hdl.handle.net/20.500.12105/7698 | |
dc.description.abstract | The packaging of proteins into discrete compartments is an essential feature for cellular efficiency. Inspired by Nature, we harness virus-like assemblies as artificial nanocompartments for enzyme-catalyzed cascade reactions. Using the negative charges of nucleic acid tags, we develop a versatile strategy to promote an efficient noncovalent co-encapsulation of enzymes within a single protein cage of cowpea chlorotic mottle virus (CCMV) at neutral pH. The encapsulation results in stable 21-22 nm sized CCMV-like particles, which is characteristic of an icosahedral T = 1 symmetry. Cryo-EM reconstruction was used to demonstrate the structure of T = 1 assemblies templated by biological soft materials as well as the extra-swelling capacity of these T = 1 capsids. Furthermore, the specific sequence of the DNA tag is capable of operating as a secondary biocatalyst as well as bridging two enzymes for co-encapsulation in a single capsid while maintaining their enzymatic activity. Using CCMV-like particles to mimic nanocompartments can provide valuable insight on the role of biological compartments in enhancing metabolic efficiency. | es_ES |
dc.description.sponsorship | We acknowledge financial support from the ERC Consolidator Grant (Protcage) and the Indonesia Endowment Fund for Education (LPDP). This work was supported in part by grants from the Spanish Ministry of Economy and Competitivity (BFU2014-55475 to JRC) and the Comunidad Autónoma de Madrid (S2013/MIT-2807 to JRC). | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | American Chemical Society (ACS) | es_ES |
dc.type.hasVersion | VoR | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject.mesh | Biocatalysis | es_ES |
dc.subject.mesh | Bromovirus | es_ES |
dc.subject.mesh | Glucose Oxidase | es_ES |
dc.subject.mesh | Nucleic Acids | es_ES |
dc.subject.mesh | Particle Size | es_ES |
dc.subject.mesh | Phosphogluconate Dehydrogenase | es_ES |
dc.subject.mesh | Phosphotransferases (Alcohol Group Acceptor) | es_ES |
dc.subject.mesh | Surface Properties | es_ES |
dc.title | Assembling Enzymatic Cascade Pathways inside Virus-Based Nanocages Using Dual-Tasking Nucleic Acid Tags | es_ES |
dc.type | journal article | es_ES |
dc.rights.license | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.identifier.pubmedID | 28055188 | es_ES |
dc.format.volume | 139 | es_ES |
dc.format.number | 4 | es_ES |
dc.format.page | 1519 | es_ES |
dc.identifier.doi | 10.1021/jacs.6b10948 | es_ES |
dc.contributor.funder | Comunidad de Madrid (España) | |
dc.contributor.funder | Ministerio de Economía y Competitividad (España) | |
dc.description.peerreviewed | Sí | es_ES |
dc.identifier.e-issn | 1520-5126 | es_ES |
dc.relation.publisherversion | https://doi.org/10.1021/jacs.6b10948 | es_ES |
dc.identifier.journal | Journal of the American Chemical Society | es_ES |
dc.repisalud.centro | ISCIII::Centro Nacional de Microbiología | es_ES |
dc.repisalud.institucion | ISCIII | es_ES |
dc.relation.projectID | info:eu-repo/grantAgreement/ES/BFU2014-55475 | es_ES |
dc.relation.projectID | info:eu-repo/grantAgreement/ES/S2013/MIT-2807 | es_ES |
dc.rights.accessRights | open access | es_ES |