Glycosylinositol phosphorylceramides from Rosa cell cultures are boron-bridged in the plasma membrane and form complexes with rhamnogalacturonan II.
Bottom Line: Using high-voltage paper electrophoresis, we showed that addition of GIPCs decreased the electrophoretic mobility of radiolabelled RG-II, suggesting formation of a GIPC-B-RG-II complex.We conclude that B plays a structural role in the plasma membrane.Finally, our results suggest a role for GIPCs in the RG-II dimerization process.
Affiliation: The Edinburgh Cell Wall Group, Institute of Molecular Plant Sciences, The University of Edinburgh, Edinburgh, EH9 3JH, UK.Show MeSH
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Mentions: In order to test whether GIPC plays a role in RG-II dimerization, we incubated GIPC with purified RG-II plus H3BO3 under conditions devised for demonstrating Pb2+-induced dimerization. After 4 h, the reaction mixture was analysed by polyacrylamide gel electrophoresis (PAGE) (Chormova et al., 2013). Some experiments showed that GIPC was able to enhance dimer formation as effectively as Pb2+in vitro (Figure5a). Other repeat experiments demonstrated a smaller effect of GIPC (Figure5b), although the dimerization rate was always higher with GIPC + H3BO3 than with H3BO3 alone.
Affiliation: The Edinburgh Cell Wall Group, Institute of Molecular Plant Sciences, The University of Edinburgh, Edinburgh, EH9 3JH, UK.