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Plant and Cell Physiology Advance Access published online on May 28, 2009
Plant and Cell Physiology, 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 e-mail: journals.permissions@oxfordjournals.org

Membrane-associated, Boron Interacting Proteins Isolated By Boronate Affinity Chromatography

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

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

Corresponding author: Dr. Monika A. Wimmer, Karlrobert-Kreiten-Str. 13, 53115 Bonn, Germany, phone ##49-228-731636; fax: ##49-228-732489; e-mail: m.wimmer{at}uni-bonn.de


  Abstract

Boron deficiency symptoms point to a role of 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 peptide mass fingerprinting.

Sixteen boron-binding membrane-associated proteins were identified in A. thaliana, and nine in Z. mays roots. Additional un-identified proteins were also present. Common to both species were the beta subunit of mitochondrial ATP synthase, several beta-glucosidases, a luminal binding protein and fructose bisphosphate aldolase. In A. thaliana, binding of these proteins to boron was significantly reduced after 4 days 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 function in plant membranes by crosslinking glycoproteins, and may be involved in their recruiting to membrane microdomains.

Keywords: affinity chromatography - Arabidopsis thaliana - boron - membrane - proteomics - Zea mays

*present Address: Institute of Plant Nutrition and Soil Science, University of Kiel, 24118 Kiel, Germany

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