A Novel Histidine-Rich CPx-ATPase from the Filamentous Cyanobacterium Oscillatoria brevis Related to Multiple-Heavy-Metal Cotolerance
AUTOR(ES)
Tong, Liu
FONTE
American Society for Microbiology
RESUMO
A novel gene related to heavy-metal transport was cloned and identified from the filamentous cyanobacterium Oscillatoria brevis. Sequence analysis of the gene (the Bxa1 gene) showed that its product possessed high homology with heavy-metal transport CPx-ATPases. The CPC motif, which is proposed to form putative cation transduction channel, was found in the sixth transmembrane helix. However, instead of the CXXC motif that is present in the N termini of most metal transport CPx-ATPases, Bxa1 contains a unique Cys-Cys (CC) sequence element and histidine-rich motifs as a putative metal binding site. Northern blotting and real-time quantitative reverse transcription-PCR showed that expression of Bxa1 mRNA was induced in vivo by both monovalent (Cu+ and Ag+) and divalent (Zn2+ and Cd2+) heavy-metal ions at similar levels. Experiments on heavy-metal tolerance in Escherichia coli with recombinant Bxa1 demonstrated that Bxa1 conferred resistance to both monovalent and divalent heavy metals. This is the first report of a CPx-ATPase responsive to both monovalent and divalent heavy metals.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=135323Documentos Relacionados
- Histidine-Rich Protein II: a Novel Approach to Malaria Drug Sensitivity Testing
- Histidine-rich glycoprotein inhibits the antiangiogenic effect of thrombospondin-1
- KpnI RFLP in the human histidine-rich glycoprotein gene
- Interaction of histidine-rich glycoprotein with fibrinogen and fibrin.
- Complex formation of platelet thrombospondin with histidine-rich glycoprotein.