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logo citeas López‐Maury, L., García‐Domínguez, M., Florencio, F. J., & Reyes, J. C. (2002, January). A two‐component signal transduction system involved in nickel sensing in the cyanobacterium Synechocystis sp. PCC 6803. Molecular Microbiology. Wiley. http://doi.org/10.1046/j.1365-2958.2002.02741.x
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Título

A two-component signal transduction system involved in nickel sensing in the cyanobacterium Synechocystis sp. PCC 6803

AutorLópez-Maury, Luis CSIC ORCID ; García-Domínguez, Mario CSIC ORCID; Florencio, Francisco J.; Reyes, José C. CSIC ORCID
FinanciadoresMinisterio de Educación, Cultura y Deporte (España)
Junta de Andalucía
Dirección General de Enseñanza Superior e Investigación Científica (España)
Fecha de publicaciónene-2002
EditorWiley-Blackwell
CitaciónMolecular Microbiology 43(1): 247-256 (2002)
ResumenIn the cyanobacterium Synechocystis sp. PCC 6803, genes for Ni2+, Co2+, and Zn2+ resistance are grouped in a 12 kb gene cluster. The nrsBACD operon is composed of four genes, which encode proteins involved in Ni2+ resistance. Upstream from nrsBACD, and in opposite orientation, a transcription unit formed by the two genes rppA and rppB has been reported previously to encode a two-component signal transduction system involved in redox sensing. In this report, we demonstrate that rppA and rppB (here redesigned nrsR and nrsS respectively) control the Ni2+-dependent induction of the nrsBACD operon and are involved in Ni2+ sensing. Thus, expression of the nrsBACD operon was not induced by Ni2+ in a nrsRS mutant strain. Furthermore, nrsRS mutant cells showed reduced tolerance to Ni2+. Whereas the nrsBACD operon is transcribed from two different promoters, one constitutive and the other dependent on the presence of Ni2+ in the medium, the nrsRS operon is transcribed from a single Ni2+-inducible promoter. The nrsRS promoter is silent in a nrsRS mutant background suggesting that the system is autoregulated. Purified full length NrsR protein is unable to bind to the nrsBACD-nrsRS intergenic region; however, an amino-terminal truncated protein that contains the DNA binding domain of NrsR binds specifically to this region. Our nrsRS mutant, which carries a deletion of most of the nrsR gene and part of the nrsS gene, does not show redox imbalance or photosynthetic gene mis-expression, contrasting with the previously reported nrsR mutant.
Versión del editorhttp://dx.doi.org/10.1046/j.1365-2958.2002.02741.x
URIhttp://hdl.handle.net/10261/270478
DOI10.1046/j.1365-2958.2002.02741.x
Identificadoresdoi: 10.1046/j.1365-2958.2002.02741.x
issn: 0950-382X
e-issn: 1365-2958
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