dc.creator | Feria Bourrellier, Ana Belén | es |
dc.creator | Valot, Benoit | es |
dc.creator | Guillot, Alain | es |
dc.creator | Ambard-Bretteville, Françoise | es |
dc.creator | Vidal, Jean | es |
dc.creator | Hodges, Michael | es |
dc.date.accessioned | 2020-07-10T09:33:44Z | |
dc.date.available | 2020-07-10T09:33:44Z | |
dc.date.issued | 2010-01 | |
dc.identifier.citation | Feria Bourrellier, A.B., Valot, B., Guillot, A., Ambard-Bretteville, F., Vidal, J. y Hodges, M. (2010). Chloroplast acetyl-CoA carboxylase activity is 2-oxoglutarate–regulated by interaction of PII with the biotin carboxyl carrier subunit. PNAS, 107 (1), 502-507. | |
dc.identifier.issn | 0027-8424 | es |
dc.identifier.issn | 1091-6490 | es |
dc.identifier.uri | https://hdl.handle.net/11441/99193 | |
dc.description.abstract | The PII protein is a signal integrator involved in the regulation of
nitrogen metabolism in bacteria and plants. Upon sensing of
cellular carbon and energy availability, PII conveys the signal by
interacting with target proteins, thereby modulating their biological activity. Plant PII is located to plastids; therefore, to identify
new PII target proteins, PII-affinity chromatography of soluble
extracts from Arabidopsis leaf chloroplasts was performed. Several proteins were retained only when Mg-ATP was present in the
binding medium and they were specifically released from the resin
by application of a 2-oxoglutarate-containing elution buffer. Mass
spectroscopy of SDS/PAGE-resolved protein bands identified the
biotin carboxyl carrier protein subunits of the plastidial acetyl-CoA
carboxylase (ACCase) and three other proteins containing a similar
biotin/lipoyl-binding motif as putative PII targets. ACCase is a key
enzyme initiating the synthesis of fatty acids in plastids. In in vitro
reconstituted assays supplemented with exogenous ATP, recombinant Arabidopsis PII inhibited chloroplastic ACCase activity, and
this was completely reversed in the presence of 2-oxoglutarate,
pyruvate, or oxaloacetate. The inhibitory effect was PII-dosedependent and appeared to be PII-specific because ACCase activity
was not altered in the presence of other tested proteins. PII
decreased the Vmax of the ACCase reaction without altering the
Km for acetyl-CoA. These data show that PII function has evolved
between bacterial and plant systems to control the carbon metabolism pathway of fatty acid synthesis in plastids. | es |
dc.format | application/pdf | es |
dc.format.extent | 6 p. | es |
dc.language.iso | eng | es |
dc.publisher | National Academy of Sciences | es |
dc.relation.ispartof | PNAS, 107 (1), 502-507. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Arabidopsis thaliana | es |
dc.subject | Biotin carboxyl carrier protein | es |
dc.subject | PII protein | es |
dc.subject | Organic acids | es |
dc.subject | Fatty acid metabolism | es |
dc.title | Chloroplast acetyl-CoA carboxylase activity is 2-oxoglutarate–regulated by interaction of PII with the biotin carboxyl carrier subunit | 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 Biología Vegetal y Ecología | es |
dc.relation.publisherversion | https://doi.org/10.1073/pnas.0910097107 | es |
dc.identifier.doi | 10.1073/pnas.0910097107 | es |
dc.journaltitle | PNAS | es |
dc.publication.volumen | 107 | es |
dc.publication.issue | 1 | es |
dc.publication.initialPage | 502 | es |
dc.publication.endPage | 507 | es |
dc.contributor.funder | Fundación Alfonso Martín Escudero. España | es |
dc.contributor.funder | Centre national de la recherche scientifique (CNRS). France | es |
dc.contributor.funder | Université de Paris | es |