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Open Access item Insights into the mechanism of activation of the phosphorylation-independent response regulator NblR. Role of residues Cys69 and Cys96

Authors:Espinosa, Javier
Lopez-Redondo, Maria-Luisa
Neira, José L.
Marina, Alberto
Contreras, Asunción
Keywords:Stress response, NblR, Cyanobacteria, Cysteine, Response regulator, Structure
Issue Date:28-Jan-2012
Publisher:Elsevier
Citation:Biochimica et Biophysica Acta - Gene Regulatory Mechanisms 1819(5): 382-90 (2012)
Abstract:Cyanobacteria respond to environmental stress conditions by adjusting their photosynthesis machinery. In Synechococcus sp. PCC 7942, phycobilisome degradation and other acclimation responses after nutrient or high light stress require activation by the phosphorylation-independent response regulator NblR. Structural modelling of its receiver domain suggested a role for Cys69 and Cys96 on activation of NblR. Here, we investigate this hypothesis by engineering Cys to Ala substitutions. In vivo and in vitro analyses indicated that mutations Cys69Ala and/or Cys96Ala have a minor impact on NblR function, structure, size, or oligomerization state of the protein, and that Cys69 and Cys96 do not seem to form disulphide bridges. Our results argue against the predicted involvement of Cys69 and Cys96 on NblR activation by redox sensing
Description:9 páginas, 8 figuras.
Publisher version (URL):http://dx,doi.org/10.1016/j.bbagrm.2012.01.007
URI:http://hdl.handle.net/10261/57397
ISSN:0006-3002
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Appears in Collections:(IBV) Artículos

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