Identification of boron-binding proteins supports a function of boron at the cell membrane

Our current understanding of boron’s roles in plants is still limited to the formation of B-rhamnogalacturonan-crosslinks in the cell wall, but deficiency symptoms in plants and animals point to additional functions of boron (B) in cell membranes. However, no membrane-bound molecules interacting with B have been isolated so far.In the present study we address the hypothesis that boron exerts a physiological function at membranes by crosslinking membrane-bound proteins.Boron-interacting membrane proteins were isolated from root microsomal preparations of arabidopsis (Arabidopsis thaliana) and maize (Zea mays) using phenylboronate affinity chromatography, subsequently separated by two-dimensional gel electrophoresis and identified using MALDI-TOF peptide mass fingerprinting.A relatively large number of B-binding membrane proteins was detected, of which sixteen (A. thaliana) and nine (Z. mays) were identified. Common to both species were the beta subunit of mitochondrial ATP synthase, several beta-glucosidases, a luminal binding protein and fructose bisphosphate aldolase. Binding of these proteins to B was significantly reduced after 5 days of B deprivation in A. thaliana. Plants grown under B deficiency also exhibited an altered protein composition of membrane microdomains. This combined with the fact that many of the B-binding proteins are components of membrane rafts, supports the hypothesis that B may indeed play a function in plant membranes by crosslinking glycoproteins, and may be involved in their recruiting to membrane microdomains