dc.creator | Saelices Gómez, Lorena | es |
dc.creator | Robles Rengel, Rocio | es |
dc.creator | Florencio Bellido, Francisco Javier | es |
dc.date.accessioned | 2018-01-18T09:46:04Z | |
dc.date.available | 2018-01-18T09:46:04Z | |
dc.date.issued | 2015 | |
dc.identifier.citation | Saelices Gómez, L., Robles Rengel, R. y Florencio Bellido, F.J. (2015). A core of three amino acids at the carboxyl-terminal region of glutamine synthetase defines its regulation in cyanobacteria. Molecular Microbiology, 96, 483-496. | |
dc.identifier.issn | 0950-382X | es |
dc.identifier.uri | https://hdl.handle.net/11441/69141 | |
dc.description.abstract | Glutamine synthetase (GS) type I is a key enzyme in nitrogen metabolism, and its activity is finely controlled by cellular carbon/nitrogen balance. In cyanobacteria, a reversible process that involves protein-protein interaction with two proteins, the inactivating factors IF7 and IF17, regulates GS. Previously, we showed that three arginine residues of IFs are critical for binding and inhibition of GS. In this work, taking advantage of the specificity of GS/IFs interaction in the model cyanobacteria Synechocystis sp. PCC 6803 and Anabaena sp. PCC 7120, we have constructed a different chimeric GSs from these two cyanobacteria. Analysis of these proteins, together with a site-directed mutagenesis approach, indicates that a core of three residues (E419, N456 and R459) is essential for the inactivation process. The three residues belong to the last 56 amino acids of the C-terminus of SynechocystisGS. A protein-protein docking modeling of SynechocystisGS in complex with IF7 supports the role of the identified core for GS/IF interaction. | es |
dc.description.sponsorship | España, MINECO BFU 2010 - 15708 and BFU 2013 - 41712 | es |
dc.description.sponsorship | Junta de Andalucía Bio - 284 | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Wiley | es |
dc.relation.ispartof | Molecular Microbiology, 96, 483-496. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Synechocystis 6803 | es |
dc.subject | Posttranscriptional Regulation | es |
dc.subject | Inactivating Factors | es |
dc.subject | Glutamine Synthetase | es |
dc.subject | Protein-Protein Interaction | es |
dc.title | A core of three amino acids at the carboxyl-terminal region of glutamine synthetase defines its regulation in cyanobacteria | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/submittedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular | es |
dc.relation.projectID | BFU 2010 - 15708 | es |
dc.relation.projectID | BFU 2013 - 41712 | es |
dc.relation.projectID | Bio - 284 | es |
dc.relation.publisherversion | http://dx.doi.org/10.1111/mmi.12950 | es |
dc.identifier.doi | 10.1111/mmi.12950 | es |
idus.format.extent | 13 p. | es |
dc.journaltitle | Molecular Microbiology | es |
dc.publication.volumen | 96 | es |
dc.publication.initialPage | 483 | es |
dc.publication.endPage | 496 | es |
dc.contributor.funder | Ministerio de Economía y Competitividad (MINECO). España | |
dc.contributor.funder | Junta de Andalucía | |