Haloferax mediterranei GlnK proteins are post-translationally modified by uridylylation

Please use this identifier to cite or link to this item: http://hdl.handle.net/10045/44400
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dc.contributorBiotecnología de Extremófilos (BIOTECEXTREM)es
dc.contributor.authorPedro Roig, Laia-
dc.contributor.authorCamacho, Mónica-
dc.contributor.authorBonete, María-José-
dc.contributor.otherUniversidad de Alicante. Departamento de Agroquímica y Bioquímicaes
dc.date.accessioned2015-01-28T13:52:36Z-
dc.date.available2015-01-28T13:52:36Z-
dc.date.issued2013-04-
dc.identifier.citationProteomics. 2013, 13(8): 1371-1374. doi:10.1002/pmic.201200465es
dc.identifier.issn1615-9853 (Print)-
dc.identifier.issn1615-9861 (Online)-
dc.identifier.urihttp://hdl.handle.net/10045/44400-
dc.description.abstractIn this work we report for the first time a post-translational modification of PII homologues from the Archaea Domain. Haloferax mediterranei is the first haloarchaea whose PII proteins have been studied, it possesses two of them (GlnK1 and GlnK2), both encoded adjacent to a gene for the ammonia transporter Amt. An approach based on 2DE, anti-GlnK immunoblot and peptide mass fingerprint (MALDI-TOF-MS) of the reactive spots showed that GlnK proteins in H. mediterranei are post-translationally uridylylated. A third spot with lower pI suggests the existence of a non-descript post-translational modification in this protein family.es
dc.description.sponsorshipThis work was supported by project BIO2008-00082 from the Spanish Ministry of Science and Innovation (MICINN), which includes funding from the European Union (“FEDER”). L.P.R. is supported by a fellowship (AP2007-02932) from the Ministry of Education.es
dc.languageenges
dc.publisherWiley-VCH Verlag GmbH & Co. KGaAes
dc.rights© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheimes
dc.subjectArchaeaes
dc.subjectGlnKes
dc.subjectHaloferaxes
dc.subjectMicrobiologyes
dc.subjectPost-translational modificationes
dc.subjectUridylylationes
dc.subject.otherBioquímica y Biología Moleculares
dc.titleHaloferax mediterranei GlnK proteins are post-translationally modified by uridylylationes
dc.typeinfo:eu-repo/semantics/articlees
dc.peerreviewedsies
dc.identifier.doi10.1002/pmic.201200465-
dc.relation.publisherversionhttp://dx.doi.org/10.1002/pmic.201200465es
dc.rights.accessRightsinfo:eu-repo/semantics/restrictedAccesses
Appears in Collections:INV - BIOTECEXTREM - Artículos de Revistas

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