Showing papers by "Klaus Palme published in 1990"

Auxin binding proteins from maize coleoptiles : purification and molecular characterization

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.

The auxin-binding-protein from maize coleoptiles.

Abstract: There is good evidence that auxin-dependent cell elongation (Lobler, Klambt (1985b) and H+ secretion (Barbier-Brygoo et al., 1989) is mediated by an auxin-binding-protein (ABP). The ABP is isolated from maize coleoptiles, purified and characterized by Lobler and Klambt (1985 a,b) and Shimomura et al. (1986). Recently cDNA clones of ABP were isolated, sequenced and further characterized (Hesse et al., 1989; Tillmann et al., 1989; Inohara et al., 1989). These reports confirmed earlier results. The pre-ABP contains a signal peptide and one glycosylation site.