TY - JOUR
T1 - The glossy1 Locus of Maize and an Epidermis-Specific cDNA from Kleinia odora Define a Class of Receptor-Like Proteins Required for the Normal Accumulation of Cuticular Waxes
AU - Hansen, Joel D.
AU - Pyee, Jaeho
AU - Xia, Yiji
AU - Wen, Tsui Jung
AU - Robertson, Donald S.
AU - Kolattukudy, Papachan E.
AU - Nikolau, Basil J.
AU - Schnable, Patrick S.
N1 - Funding information:
This work was supported in part by National Science Foundation grant nos. IBN-9316832 (to P.S.S. and B.J.N.) and IBN9318544 (to P.E.K.), The Herman Frasch Foundation grant no. 322-HF92 (to B.J.N.), Department of Energy grant no. DE-FG02-93 ER 20109 (to P.E.K.), and by the Iowa State University Office of Biotechnology (to P.S.S. and B.J.N.). This is journal paper no. J-16898 of the Iowa Agriculture and Home Economics Experiment Station, project nos. 2913 and 2882, and is supported by the Hatch Act and State of Iowa funds.
Publisher copyright:
©1997 by American Society of Plant Biologists
PY - 1997/4
Y1 - 1997/4
N2 - Mutations at the glossy1 (gl1) locus of maize (Zea mays L.) quantitatively and qualitatively affect the deposition of cuticular waxes on the surface of seedling leaves. The gl1 locus has been molecularly cloned by transposon tagging with the Mutator transposon system. The epi23 cDNA was isolated by subtractive hybridization as an epidermis-specific mRNA from Senecio odora (Kleinia odora). The deduced amino acid sequence of the GL1 and EPI23 proteins are very similar to each other and to two other plant proteins in which the sequences were deduced from their respective mRNAs. These are the Arabidopsis CER1 protein, which is involved in cuticular wax deposition on siliques, stems, and leaves of that plant, and the protein coded by the rice expressed sequence tag RICS2751A. All four proteins are predicted to be localized in a membrane via a common NH2-terminal domain, which consists of either five or seven membrane-spanning helices. The COOH-terminal portion of each of these proteins, although less conserved, is predicted to be a water-soluble, globular domain. These sequence similarities indicate that these plant orthologs may belong to a superfamily of membrane-bound receptors that have been extensively characterized from animals, including the HIV co-receptor fusin (also termed CXCR4).
AB - Mutations at the glossy1 (gl1) locus of maize (Zea mays L.) quantitatively and qualitatively affect the deposition of cuticular waxes on the surface of seedling leaves. The gl1 locus has been molecularly cloned by transposon tagging with the Mutator transposon system. The epi23 cDNA was isolated by subtractive hybridization as an epidermis-specific mRNA from Senecio odora (Kleinia odora). The deduced amino acid sequence of the GL1 and EPI23 proteins are very similar to each other and to two other plant proteins in which the sequences were deduced from their respective mRNAs. These are the Arabidopsis CER1 protein, which is involved in cuticular wax deposition on siliques, stems, and leaves of that plant, and the protein coded by the rice expressed sequence tag RICS2751A. All four proteins are predicted to be localized in a membrane via a common NH2-terminal domain, which consists of either five or seven membrane-spanning helices. The COOH-terminal portion of each of these proteins, although less conserved, is predicted to be a water-soluble, globular domain. These sequence similarities indicate that these plant orthologs may belong to a superfamily of membrane-bound receptors that have been extensively characterized from animals, including the HIV co-receptor fusin (also termed CXCR4).
UR - http://www.scopus.com/inward/record.url?scp=0031128012&partnerID=8YFLogxK
U2 - 10.1104/pp.113.4.1091
DO - 10.1104/pp.113.4.1091
M3 - Journal article
C2 - 9112770
AN - SCOPUS:0031128012
SN - 0032-0889
VL - 113
SP - 1091
EP - 1100
JO - Plant Physiology
JF - Plant Physiology
IS - 4
ER -