Regulation of ammonium assimilation in Haloferax mediterranei: Interaction between glutamine synthetase and two GlnK proteins

Please use this identifier to cite or link to this item:
Información del item - Informació de l'item - Item information
Title: Regulation of ammonium assimilation in Haloferax mediterranei: Interaction between glutamine synthetase and two GlnK proteins
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: GlnK | PII | Haloferax mediterranei | Nitrogen metabolism regulation | 2-oxoglutarate | Glutamine synthetase
Knowledge Area: Bioquímica y Biología Molecular
Issue Date: Jan-2013
Publisher: Elsevier
Citation: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 2013, 1834(1): 16-23. doi:10.1016/j.bbapap.2012.10.006
Abstract: GlnK proteins belong to the PII superfamily of signal transduction proteins and are involved in the regulation of nitrogen metabolism. These proteins are normally encoded in an operon together with the structural gene for the ammonium transporter AmtB. Haloferax mediterranei possesses two genes encoding for GlnK, specifically, glnK1 and glnK2. The present study marks the first investigation of PII proteins in haloarchaea, and provides evidence for the direct interaction between glutamine synthetase and both GlnK1 and GlnK2. Complex formation between glutamine synthetase and the two GlnK proteins is demonstrated with pure recombinant protein samples using in vitro activity assays, gel filtration chromatography and western blotting. This protein–protein interaction increases glutamine synthetase activity in the presence of 2-oxoglutarate. Separate experiments that were carried out with GlnK1 and GlnK2 produced equivalent results.
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”). LPR is supported by a fellowship (AP2007-02932) from the Ministry of Education.
ISSN: 1570-9639 (Print) | 1878-1454 (Online)
DOI: 10.1016/j.bbapap.2012.10.006
Language: eng
Type: info:eu-repo/semantics/article
Peer Review: si
Publisher version:
Appears in Collections:INV - BIOTECEXTREM - Artículos de Revistas

Files in This Item:
Files in This Item:
File Description SizeFormat 
Thumbnail2013_Pedro-Roig_etal_BBA-PAP_final.pdfVersión final (acceso restringido)1,39 MBAdobe PDFOpen    Request a copy

Items in RUA are protected by copyright, with all rights reserved, unless otherwise indicated.