Molecular cloning and characterization of plant genes encoding novel peroxisomal molybdoenzymes of the sulphite oxidase family
doi: 10.1093/jxb/erf042
pmid: 12147736
Molecular cloning and characterization of plant genes encoding novel peroxisomal molybdoenzymes of the sulphite oxidase family
The Arabidopsis AtMCP and rice OsMCP genes which encode proteins highly homologous to molybdoenzymes of the sulphite oxidase family were isolated and characterized. Both proteins seemed to possess only a molybdenum cofactor as the redox centre, unlike all the other eukaryotic molybdoenzymes. Putative MCP orthologues were identified in 17 plant species, indicating that MCPs are widely distributed over the plant kingdom [corrected]. An analysis using a green fluorescent protein fusion showed that AtMCP possesses a peroxisomal targeting signal at its C-terminus. Putative peroxisomal targeting signals were also found in all plant MCPs, suggesting the existence of a new redox pathway in this organelle.
Molybdenum, Sequence Homology, Amino Acid, Recombinant Fusion Proteins, Green Fluorescent Proteins, Molecular Sequence Data, Arabidopsis, Oryza, Luminescent Proteins, Peroxisomes, Oxidoreductases Acting on Sulfur Group Donors, Amino Acid Sequence, Cloning, Molecular, Plant Proteins
Molybdenum, Sequence Homology, Amino Acid, Recombinant Fusion Proteins, Green Fluorescent Proteins, Molecular Sequence Data, Arabidopsis, Oryza, Luminescent Proteins, Peroxisomes, Oxidoreductases Acting on Sulfur Group Donors, Amino Acid Sequence, Cloning, Molecular, Plant Proteins
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