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Purification of the Trehalase GMTRE1 from Soybean Nodules and Cloning of Its cDNA. GMTRE1 Is Expressed at a Low Level in Multiple Tissues1

Roger A. Aeschbacher*, Joachim Müller, Thomas Boller, and Andres Wiemken

Botanisches Institut, Universität Basel, Hebelstrasse 1, CH-4056 Basel, Switzerland

Trehalose (alpha -D-glucopyranosyl-1,1-alpha -D-glucopyranoside), a disaccharide widespread among microbes and lower invertebrates, is generally believed to be nonexistent in higher plants. However, the recent discovery of Arabidopsis genes whose products are involved in trehalose synthesis has renewed interest in the possibility of a function of trehalose in higher plants. We previously showed that trehalase, the enzyme that degrades trehalose, is present in nodules of soybean (Glycine max [L.] Merr.), and we characterized the enzyme as an apoplastic glycoprotein. Here we describe the purification of this trehalase to homogeneity and the cloning of a full-length cDNA encoding this enzyme, named GMTRE1 (G. max trehalase 1). The amino acid sequence derived from the open reading frame of GMTRE1 shows strong homology to known trehalases from bacteria, fungi, and animals. GMTRE1 is a single-copy gene and is expressed at a low but constant level in many tissues.

1   This work was supported by grants from the Swiss National Science Foundation (no. 3100-042535.94 to A.W. and no. 3100-040837.94 to T.B.).
*   Corresponding author; e-mail aeschbacher{at}ubaclu.unibas.ch; fax 41-61-267-23-30.

Plant Physiol. (1999) 119: 489-496
Copyright Clearance Center:   0032-0889/99/119//08
© 1999 American Society of Plant Physiologists




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