The nitrogen interaction network in Synechococcus WH5701, a cyanobacterium with two PipX and two PII-like proteins

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Title: The nitrogen interaction network in Synechococcus WH5701, a cyanobacterium with two PipX and two PII-like proteins
Authors: Laichoubi, Karim Boumediene | Beez, Sabine | Espinosa Manzano, Javier | 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 Tuebingen. Lehrstuhl fur Mikrobiologie, Organismische Interaktionen
Keywords: Synechococcus | PipX
Knowledge Area: Genética
Date Created: Dec-2010
Issue Date: Apr-2011
Publisher: Society for General Microbiology
Citation: LAICHOUBI, Karim Boumediene, et al. “The nitrogen interaction network in Synechococcus WH5701, a cyanobacterium with two PipX and two PII-like proteins”. Microbiology. 157 (2011). ISSN 1350-0872, pp. 1220-1228
Abstract: Nitrogen regulation involves the formation of different types of protein complexes between signal transducers and their transcriptional or metabolic targets. In oxygenic phototrophs, the signal integrator PII activates the enzyme N-acetyl-l-glutamate kinase (NAGK) by complex formation. PII also interacts with PipX, a protein with a tudor-like domain that mediates contacts with PII and with the transcriptional regulator NtcA, to which it binds to increase its activity. Here, we use a combination of in silico, yeast two-hybrid and in vitro approaches to investigate the nitrogen regulation network of Synechococcus WH5701, a marine cyanobacterium with two PII (GlnB_A and GlnB_B) and two PipX (PipX_I and PipX_II) proteins. Our results indicate that GlnB_A is functionally equivalent to the canonical PII protein from Synechococcus elongatus. GlnB_A interacted with PipX and NAGK proteins and stimulated NAGK activity, counteracting arginine inhibition. GlnB_B had only a slight stimulatory effect on NAGK activity, but its potential to bind effectors and form heterotrimers in Synechococcus WH5701 indicates additional regulatory functions. PipX_II, and less evidently PipX_I, specifically interacted with GlnB_A and NtcA, supporting a role for both Synechococcus WH5701 PipX proteins in partner swapping with GlnB_A and NtcA.
Sponsor: This work was supported by grants from Ministerio de Ciencia e Innovación (BFU2009-07371) and Ministerio de Educación y Ciencia (HA2007-0074).
URI: http://hdl.handle.net/10045/17724
ISSN: 1350-0872 (Print) | 1465-2080 (Online)
DOI: 10.1099/mic.0.047266-0
Language: eng
Type: info:eu-repo/semantics/article
Peer Review: si
Publisher version: http://dx.doi.org/10.1099/mic.0.047266-0
Appears in Collections:INV - TSB - Artículos de Revistas

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