Reference "Molecular cloning and structural analysis of a gene from Zea mays (L.) coding for a putative receptor for the plant hormone auxin"

Reference ID

7082

Title

Molecular cloning and structural analysis of a gene from Zea mays (L.) coding for a putative receptor for the plant hormone auxin

Source

The EMBO journal, 1989, vol. 8, pp. 2453-2461

Authors (10)

Hesse-T	Feldwisch-J
Balshusemann-D	Bauw-G
Puype-M	Vandekerckhove-J
Lobler-M	Klambt-D
Schell-J	Palme-K

Abstract

The major auxin-binding protein from maize coleoptiles was purified to
homogeneity. The protein has an apparent mol. wt of 22 kd and binds 1-
naphthylacetic acid with a KD of 2.40 x 10(-7) M. Additional antigenically
related proteins, present in very low amounts, could be demonstrated in maize
coleoptiles using immunodetection. Extensive protein sequence analysis of the
major auxin-binding protein allowed the construction of several synthetic
oligonucleotide probes which were used to isolate a cDNA coding for this
protein. The cDNA corresponds to a mRNA with a 3'-poly(A)+ sequence and a
single, long open reading frame of 603 bases. The open reading frame, starting
34 residues from the 5' end of the cDNA, predicts a 21,990 Dalton protein of 201
amino acids. Comparison of this deduced amino acid sequence with the partial
amino acid sequences of purified auxin-binding protein, revealed a perfect
match, involving a total of 53 amino acid residues. The primary amino acid
sequence includes a 38-amino-acid-long N-terminal hydrophobic leader sequence
which could represent a signal for translocation of this protein to the
endoplasmic reticulum. An additional signal is located at the C-terminal end,
consisting of the amino acids KDEL known to be responsible for preventing
secretion of proteins from the lumen of the endoplasmic reticulum in eucaryotic
cells. The primary sequence contains a N-glycosylation site (-asp133-thr-thr-).
This site was found to be glycosylated by a high-mannose-type
oligosaccharide.(ABSTRACT TRUNCATED AT 250 WORDS)