Volume 254, Issue 1 pp. 63-70

Identification of a Ferric uptake regulator from Microcystis aeruginosa PCC7806

Beatriz Martin-Luna

Beatriz Martin-Luna

Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, and Biocomputation and Complex Systems Physics Institute, Universidad de Zaragoza, Zaragoza, Spain

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Jose A. Hernandez

Jose A. Hernandez

Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, and Biocomputation and Complex Systems Physics Institute, Universidad de Zaragoza, Zaragoza, Spain

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M. Teresa Bes

M. Teresa Bes

Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, and Biocomputation and Complex Systems Physics Institute, Universidad de Zaragoza, Zaragoza, Spain

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Maria F. Fillat

Maria F. Fillat

Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, and Biocomputation and Complex Systems Physics Institute, Universidad de Zaragoza, Zaragoza, Spain

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M. Luisa Peleato

M. Luisa Peleato

Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, and Biocomputation and Complex Systems Physics Institute, Universidad de Zaragoza, Zaragoza, Spain

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First published: 15 November 2005
Citations: 4
Correspondence: M. Luisa Peleato, Departamento de Bioquímica y Biología Molecular y Celular, Facultad de Ciencias, Universidad de Zaragoza, 50009 Zaragoza, Spain. Tel.: +34 976 762479; fax: +34 976 762123; e-mail: [email protected]

Editor: Skorn Mongkolsuk

Present address: Jose A. Hernandez, Plant and Microbial Biology Department, 211 Koshland Hall, University of California at Berkeley, 94720 Berkeley, CA, USA.

Abstract

Ferric uptake regulator (Fur) proteins are widely recognized as repressors that in many prokaryotes regulate a large number of genes involved in iron homeostasis and oxidative stress response. In our study, we were able to identify the complete sequence of the fur gene from Microcystis aeruginosa using inverse-polymerase chain reaction. DNA sequence analysis confirmed the presence of a 183 amino-acid open reading frame that showed high identity with Fur proteins reported for cyanobacteria. The recombinant Fur protein has been purified and electrophoretical mobility shift assays shown to be active. Mn2+ and dithiothreitol enable Fur to bind to its promoter, with dithiothreitol being more potent. The expression of Fur in Microcystis was induced about twofold in iron-deficient conditions.

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