Reference "Auxin-binding protein located in the endoplasmic reticulum of maize shoots: molecular cloning and complete primary structure"

Reference ID

7084

Title

Auxin-binding protein located in the endoplasmic reticulum of maize shoots: molecular cloning and complete primary structure

Source

Proceedings of the National Academy of Sciences of the United States of America, 1989, vol. 86, pp. 3564-3568

Authors (4)

Inohara-N	Shimomura-S
Fukui-T	Futai-M

Abstract

We previously purified an auxin-binding protein (ABP) from the microsomal
fraction of maize shoots (Zea mays L. cv. Golden Cross Bantam). In the present
study cDNA clones derived from mRNAs encoding the ABP were isolated and
sequenced. The nucleotide sequence of the 822-base-pair cDNA includes a 603-base-
pair open reading frame. RNA blot hybridization analysis indicated a single mRNA
species of approximately 1.0 kilobase. The predicted precursor of ABP is
composed of 201 amino acid residues and has a molecular weight of 21,976. The
NH2-terminal sequence of 38 residues is hydrophobic and may be a signal peptide
for translocation of the ABP across the membrane of the endoplasmic reticulum.
The mature ABP, composed of 163 residues with a molecular weight of 18,352,
contains a potential N-glycosylation site (Asn-Thr-Thr), and the COOH-terminal
tetrapeptide (Lys-Asp-Glu-Leu) may be a signal for retention of the ABP in the
lumen of the endoplasmic reticulum.