Haloferax mediterranei GlnK proteins are post-translationally modified by uridylylation

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Title: Haloferax mediterranei GlnK proteins are post-translationally modified by uridylylation
Authors: Pedro Roig, Laia | Camacho, Mónica | Bonete, María-José
Research Group/s: Biotecnología de Extremófilos (BIOTECEXTREM)
Center, Department or Service: Universidad de Alicante. Departamento de Agroquímica y Bioquímica
Keywords: Archaea | GlnK | Haloferax | Microbiology | Post-translational modification | Uridylylation
Knowledge Area: Bioquímica y Biología Molecular
Issue Date: Apr-2013
Publisher: Wiley-VCH Verlag GmbH & Co. KGaA
Citation: Proteomics. 2013, 13(8): 1371-1374. doi:10.1002/pmic.201200465
Abstract: In 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.
Sponsor: This 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.
URI: http://hdl.handle.net/10045/44400
ISSN: 1615-9853 (Print) | 1615-9861 (Online)
DOI: 10.1002/pmic.201200465
Language: eng
Type: info:eu-repo/semantics/article
Rights: © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Peer Review: si
Publisher version: http://dx.doi.org/10.1002/pmic.201200465
Appears in Collections:INV - BIOTECEXTREM - Artículos de Revistas

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