Isolation of a French bean (Phaseolus vulgaris L.) homolog to the beta-glucan elicitor-binding protein of soybean (Glycine max L.).
A high-affinity membrane-bound beta-glucan elicitor-binding protein has been purified from microsomal preparations of French bean (Phaseolus vulgaris L.) roots. A 5900-fold purification was achieved by affinity chromatography of functionally solubilized membrane proteins. The beta-glucan-binding protein had an apparent molecular mass of 78 kDa when subjected to SDS-PAGE. Western blot analysis showed specific crossreactivity of this French bean protein with an antiserum raised against a synthetic peptide representing an internal 15 amino acid fragment of the beta-glucan-binding protein from soybean. Northern blot analysis with a cDNA probe of the soybean beta-glucan-binding protein gene revealed a crosshybridizing transcript of 2.4 kb in French bean. These results indicate that the beta-glucan-binding proteins of French bean and soybean are conserved homologs involved in beta-glucan elicitor recognition.
Mithöfer
A
A
Botanisches Institut der Universität, Menzinger Str. 67, D-80638, Munich, Germany. amithoef@botanik.biologie.uni-muenchen.de
Fliegmann
J
J
Ebel
J
J
D002352:Carrier Proteins / Q000302:isolation & purification*; D007887:Fabaceae / Q000737:chemistry*; D005936:Glucans / Q000737:chemistry*; D007425:Intracellular Membranes / Q000737:chemistry; D037102:Lectins; D008861:Microsomes / Q000737:chemistry; D010946:Plants, Medicinal; D013025:Glycine max / Q000737:chemistry*
D002352:Carrier Proteins; D005936:Glucans; D037102:Lectins; C037937:glucan-binding proteins