Proteomics is the study of all proteins from a living organism. The most advanced approach is the use of mass spectrometry to study whole cell/tissue protein content and modifications (Haynes and Yates 2000). The method has also been used to analyze proteins in biological complexes (Link et al. 1999). Although this technology is very new and requires sophisticated equipment and technical expertise, it offers a more realistic view of the physiology of the cell at a given point in time. Many studies that have traced RNA expression as a means to identify important genes in a biological process have led to disappointing results when the gene(s) is disrupted (Basse et al. 2000; Giaever et al. 2002; Timberlake and Marshall 1988). Furthermore, redundancy in gene function can confound this type of study. Analysis of the proteome can distinguish which family member is made and modifications that it may have undergone.
Initial studies on the identification of membrane proteins from arbuscular mycorrhizas formed between M. truncatula and Glomus versiforme led to the identification several protein from microsomes fractionated from mycorrhizal roots using 2D polyacrylamide gel electrophoresis and MALDI-TOF-MS (Mussa et al. 2002). Spectra of the four proteins identified were queried against the EST (expressed sequence tag) database of M. truncatulu, and good matches were found with calreticulin, nonseed lectins and an ion channel. These early results are promising, as a homolog of the nonseed lectins is known to be part of the pea nodule where it is thought to function as a storage protein. A similar relationship at this location of the root might exist between the plant and fungus at the arbuscular membrane.
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