Auxin binding proteins from maize coleoptiles: purification and molecular characterization.

K Palme, J Feldwisch, T Hesse, G Bauw, M Puype, J Vandekerchkhove, J Schell

Index: Symp. Soc. Exp. Biol. 44 , 299-313, (1990)

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Abstract

To understand precisely the mechanisms by which hormones like auxins regulate plant differentiation and development, it is essential to isolate putative hormone receptors. We have purified the major auxin binding protein from maize coleoptiles to homogeneity. The protein has an apparent molecular weight of 22,000 Da and binds 1-naphthylacetic acid with a KD of 2.4 x 10(-7) M. Protein sequence analysis allowed the construction of oligonucleotide probes to isolate a corresponding cDNA coding for this protein. The open reading frame of this cDNA predicts a protein of 201 amino acids and 21,990 Da in size. The amino acid sequence includes a cleavable N-terminal signal sequence and a C-terminal signal element consisting of the amino acids Lys Asp Glu Leu known to be responsible for preventing secretion of proteins from the lumen of the endoplasmic reticulum.