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Plant and Cell Physiology Advance Access originally published online on May 28, 2009
Plant and Cell Physiology 2009 50(7):1292-1304; doi:10.1093/pcp/pcp073
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© The Author 2009. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

This article appears in the following Plant and Cell Physiology issue: Special Issue Articles: Omics and Bioinformatics [View the issue table of contents]

Membrane-Associated, Boron-Interacting Proteins Isolated by Boronate Affinity Chromatography

Monika A. Wimmer1,*, Günter Lochnit2, Elias Bassil3, Karl H. Mühling4,5 and Heiner E. Goldbach1

1Institute of Crop Science and Resource Conservation, University of Bonn, D-53115 Bonn, Germany
2Institute of Biochemistry, Protein Analytics, University of Giessen, D-35392 Giessen, Germany
3Plant Science Department, University of California at Davis, CA 95616, USA
4Institute of Plant Nutrition, University of Giessen, D-35392 Giessen, Germany

*Corresponding author: E-mail, m.wimmer{at}uni-bonn.de; Fax, +49-228-732489.


  Abstract

Boron deficiency symptoms point to a role for boron in plant membranes, but the molecular partners interacting with boron have not yet been identified. The objective of the present study was to isolate and identify membrane-associated proteins with an ability to interact with boron. Boron-interacting 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 (matrix-assisted laser desorption ionization-time of flight) peptide mass fingerprinting. Twenty-six boron-binding membrane-associated proteins were identified in A. thaliana, and nine in Z. mays roots. Additional uniden-tified proteins were also present. Common to both species were the β-subunit of mitochondrial ATP synthase, several β-glucosidases, a luminal-binding protein and fructose bisphosphate aldolase. In A. thaliana, binding of these proteins to boron was significantly reduced after 4 d of boron deprivation. The relatively high number of diverse proteins identified as boron interacting, many of which are usually enriched in membrane microdomains, supports the hypothesis that boron plays a role in plant membranes by cross-linking glycoproteins, and may be involved in their recruitment to membrane microdomains.

Keywords: Affinity chromatography - Arabidopsis thaliana - Boron - Membrane - Proteomics - Zea mays

Abbreviations: ASB14, amidosulfobetaine-14, 3-[N,N-dimethyl(3-myristoylaminopropyl) ammonio] propanesulfonate; B, boron; BSA, bovine serum albumin; CHAPS, 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate hydrate; 2-DE, two-dimensional gel electrophoresis; DTT, dithiothreitol; GPI, glycosylphosphatidylinositol; BiP2, luminal-binding protein 2; MALDI-TOF, matrix-assisted laser desorption ionization-time of flight; MBP, myrosinase-binding protein; MS, mass spectrometry; PBA, phenylboronic acid; POD, peroxidase; PBP, Pyk10-binding protein; RGII, rhamnogalacturonan II; TX100, Triton X-100.

5Present address: Institute of Plant Nutrition and Soil Science, University of Kiel, D-24118 Kiel, Germany.

(Received March 30, 2009; Accepted May 21, 2009)
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