Poster: Proteomics

Abs # 963: Analysis Of The A. thaliana Ferredoxin Proteome

Presenter:	Hanke, Guy T, guyhanke@yahoo.co.uk
Authors	Hanke, Guy T (A)   Kimata-Ariga, Yoko  (A)   Hase, Toshiharu  (A)
Affiliations:	(A): Institute for Protein Research, Osaka University

Completion of the A. thaliana genome revealed that many well characterised proteins are represented by surprisingly large numbers of genes. Part of the 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, phytochrome synthesis and redox regulation. The purpose of this project is to assign specific function to the varied members of the A. thaliana proteome. We have purified recombinant A. thaliana Fd proteins, measured their redox potential, and analysed physical, electron transfer, and protein interaction properties. This information indicates specific functions for separate iso-proteins and may be applicable to the metabolism of all higher plants.