Effects of spontaneous mutations in PipX functions and regulatory complexes on the cyanobacterium Synechococcus elongatus strain PCC 7942

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Title: Effects of spontaneous mutations in PipX functions and regulatory complexes on the cyanobacterium Synechococcus elongatus strain PCC 7942
Authors: Espinosa Manzano, Javier | Castells Rico, Miguel Ángel | Laichoubi, Karim Boumediene | Forchhammer, Karl | Contreras, Asunción
Research Group/s: Transducción de Señales en Bacterias
Center, Department or Service: Universidad de Alicante. Departamento de Fisiología, Genética y Microbiología | University Tübingen. Lehrstuhl für Mikrobiologie, Organismische Interaktionen
Keywords: Cyanobacteria
Knowledge Area: Genética
Date Created: 2010
Issue Date: 2010
Publisher: Society for General Microbiology
Citation: ESPINOSA MANZANO, Javier, et al. “Effects of spontaneous mutations in PipX functions and regulatory complexes on the cyanobacterium Synechococcus elongatus strain PCC 7942”. Microbiology. 156 (2010). ISSN 1350-0872, pp. 1517-1526
Abstract: In Synechococcus elongatus sp. PCC 7942, PipX forms complexes with PII, a protein found in all three domains of life as an integrator of signals of the nitrogen and carbon balance, and with the cyanobacterial nitrogen regulator NtcA. We recently showed that previous inactivation of pipX facilitates subsequent inactivation of the glnB gene. Here, we show that the three spontaneous pipX point mutations pipX-92delT, pipX160C>T and pipX194T>A, initially found in different glnB strains, are indeed suppressor mutations. When these mutations were reconstructed in the wild-type background, the glnB gene could be efficiently inactivated. Furthermore, the point mutations have different effects on PipX levels, coactivation of NtcA-dependent genes and protein–protein interactions. Further support for an in vivo role of PipX–PII complexes is provided by interaction analysis with the in vivo-generated PIIT-loop+7 protein, a PII derivative unable to interact with its regulatory target N-acetyl-L-glutamate kinase, but which retains the ability to bind to PipX. The implications of these results are discussed.
Sponsor: This work was supported by grants BFU2006-12424, BFU2009-07374, ACOMP06/083, PR2009-0378 and HA2007-0074. M.A.C. is the recipient of a predoctoral fellowship from the Universidad de Alicante.
URI: http://hdl.handle.net/10045/15133
ISSN: 1350-0872 (Print) | 1465-2080 (Online)
DOI: 10.1099/mic.0.037309-0
Language: eng
Type: info:eu-repo/semantics/article
Rights: This is an author manuscript that has been accepted for publication in Microbiology, copyright Society for General Microbiology, but has not been copy-edited, formatted or proofed. Cite this article as appearing in Microbiology. This version of the manuscript may not be duplicated or reproduced, other than for personal use or within the rule of 'Fair Use of Copyrighted Materials' (section 17, Title 17, US Code), without permission from the copyright owner, Society for General Microbiology. The Society for General Microbiology disclaims any responsibility or liability for errors or omissions in this version of the manuscript or in any version derived from it by any other parties. The final copy-edited, published article, which is the version of record, can be found at http://mic.sgmjournals.org, and is freely available without a subscription.
Peer Review: si
Publisher version: http://dx.doi.org/10.1099/mic.0.037309-0
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