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Gene expression study of the flavodi-iron proteins from the cyanobacterium Synechocystis sp. PCC6803.

Authors
  • Gonçalves, Vera L1
  • Saraiva, Lígia M
  • Teixeira, Miguel
  • 1 Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República (EAN), 2780-157 Oeiras, Portugal. , (Portugal)
Type
Published Article
Journal
Biochemical Society Transactions
Publisher
Portland Press
Publication Date
Jan 01, 2011
Volume
39
Issue
1
Pages
216–218
Identifiers
DOI: 10.1042/BST0390216
PMID: 21265776
Source
Medline
License
Unknown

Abstract

The flavodi-iron proteins, also named FDPs, are an extensive family of enzymes able to reduce dioxygen to water and/or nitric oxide to nitrous oxide. These proteins are formed by a metallo-β-lactamase-like module with a di-iron catalytic site fused to a flavodoxin-like module bearing an FMN. However, in cyanobacteria, which are oxygenic photosynthetic organisms widespread in Nature, FDPs have an extra NAD(P)H:flavin reductase-like domain as a C-terminal extension. Interestingly, cyanobacteria contain more than one gene encoding FDP-like proteins, with the genome of Synechocystis sp. PCC6803 containing four genes coding for putative FDPs. However, the function of those proteins remains unclear. In the present study, we have analysed the expression profile of these genes under oxidative and nitrosative stress conditions. The results indicate that one of the flavodi-iron genes, the so-called flv1, is induced in cells exposed to nitrosative stress. By conducting a broad analysis on the primary sequences of FDPs, we have identified that the FDPs of cyanobacteria and oxygenic photosynthetic eukaryotes may be divided into multiple types (1-12), according to the amino acid residues of the di-iron catalytic site.

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