Abstract
Completion of the A. thaliana genome revealed that many well characterised proteins are represented by large numbers of genes. One challenge facing post genomic biology is to establish if this variety corresponds to redundancy, or whether the separate gene products have specialised functions. One such family of genes is that coding for ferredoxin (Fd). Fd is a 2Fe2S electron transport protein that donates electrons to many plastid enzymes essential for cellular processes, including nitrogen assimilation, sulphur assimilation, amino acid synthesis, fatty acid synthesis and redox regulation. The purpose of this project is to assign specific function to the varied members of the A. thalaiana proteome. We have purified recombinant A. thaliana Fd proteins and analysed their physical, electron transfer and protein interaction properties. This information indicates specific functions for separate proteins and may be applicable to the redox metabolism of all higher plants.
