dc.creator | Pérez-Mendoza, Daniel | es |
dc.creator | Rodríguez Carvajal, Miguel Ángel | es |
dc.creator | Romero-Jiménez, Lorena | es |
dc.creator | Araujo Farias, Gabriela de | es |
dc.creator | Lloret, Javier | es |
dc.creator | Trinidad Gallegos, Maria | es |
dc.creator | Sanjuan, Juan | es |
dc.date.accessioned | 2018-01-18T15:52:22Z | |
dc.date.available | 2018-01-18T15:52:22Z | |
dc.date.issued | 2015 | |
dc.identifier.citation | Pérez-Mendoza, D., Rodríguez-Carvajal, M.Á., Romero-Jiménez, L., De Araujo Farias, G., Lloret, J., Trinidad Gallegos, M. y Sanjuan, J. (2015). Novel mixed-linkage β-glucan activated by c-di-GMP in Sinorhizobium meliloti. Proceedings of the National Academy of Sciences of the United States of America, 112 (7), E757-E765. | |
dc.identifier.issn | 0027-8424 | es |
dc.identifier.uri | https://hdl.handle.net/11441/69183 | |
dc.description.abstract | An artificial increase of cyclic diguanylate (c-di-GMP) levels in Sinorhizobium meliloti 8530, a bacterium that does not carry known cellulose synthesis genes, leads to overproduction of a substance that binds the dyes Congo red and calcofluor. Sugar composition and methylation analyses and NMR studies identified this compound as a linear mixed-linkage (1→3)(1→4)-β-D-glucan (ML β-glucan), not previously described in bacteria but resembling ML β-glucans found in plants and lichens. This unique polymer is hydrolyzed by the specific endoglucanase lichenase, but, unlike lichenan and barley glucan, it generates a disaccharidic →4)-β-DGlcp-(1→3)-β-D-Glcp-(1→ repeating unit. A two-gene operon bgsBA required for production of this ML β-glucan is conserved among several genera within the order Rhizobiales, where bgsA encodes a glycosyl transferase with domain resemblance and phylogenetic relationship to curdlan synthases and to bacterial cellulose synthases. ML β-glucan synthesis is subjected to both transcriptional and posttranslational regulation. bgsBA transcription is dependent on the exopolysaccharide/quorum sensing ExpR/SinI regulatory system, and posttranslational regulation seems to involve allosteric activation of the ML β-glucan synthase BgsA by c-di-GMP binding to its C-terminal domain. To our knowledge, this is the first report on a linear mixed-linkage (1→3)(1→4)-β-glucan produced by a bacterium. The S. meliloti ML β-glucan participates in bacterial aggregation and biofilm formation and is required for efficient attachment to the roots of a host plant, resembling the biological role of cellulose in other bacteria. | es |
dc.description.sponsorship | Ministerio de Economía y Competittividad BIO2011-23032 | es |
dc.description.sponsorship | Junta de Andalucía P10-CVI-5800 | es |
dc.description.sponsorship | Consejo Superior de Investigaciones Científicas 201440E026 | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | National Academy of Sciences | es |
dc.relation.ispartof | Proceedings of the National Academy of Sciences of the United States of America, 112 (7), E757-E765. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Cyclic diguanylate | es |
dc.subject | Exopolysaccharides | es |
dc.subject | Plant-microbe interactions | es |
dc.title | Novel mixed-linkage β-glucan activated by c-di-GMP in Sinorhizobium meliloti | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Química Orgánica | es |
dc.relation.publisherversion | http://dx.doi.org/10.1073/pnas.1421748112 | es |
dc.identifier.doi | 10.1073/pnas.1421748112 | es |
idus.format.extent | 9 | es |
dc.journaltitle | Proceedings of the National Academy of Sciences of the United States of America | es |
dc.publication.volumen | 112 | es |
dc.publication.issue | 7 | es |
dc.publication.initialPage | E757 | es |
dc.publication.endPage | E765 | es |