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PLANT PHYSIOLOGY , Vol 105, Issue 1 35-45, Copyright © 1994 by American Society of Plant Biologists
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MOLECULAR BIOLOGY AND GENE REGULATION |
Tissue-Specific Expression of a Gene Encoding a Cell Wall-Localized Lipid Transfer Protein from Arabidopsis
S. Thoma, U. Hecht, A. Kippers, J. Botella, S. De Vries and C. Somerville
Michigan State University-Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824 (S.T., U.H., J.B., C.S.)
Nonspecific lipid transfer proteins (LTPs) from plants are characterized by
their ability to stimulate phospholipid transfer between membranes in
vitro. However, because these proteins are generally located outside of the
plasma membrane, it is unlikely that they have a similar role in vivo. As a
step toward identifying the function of these proteins, one of several LTP
genes from Arabidopsis has been cloned and the expression pattern of the
gene has been examined by analysis of the tissue specificity of
[beta]-glucuronidase (GUS) activity in transgenic plants containing LTP
promoter-GUS fusions and by in situ mRNA localization. The LTP1 promoter
was active early in development in protoderm cells of embryos, vascular
tissues, lignified tips of cotyledons, shoot meristem, and stipules. In
adult plants, the gene was expressed in epidermal cells of young leaves and
the stem. In flowers, expression was observed in the epidermis of all
developing inflorescence and flower organ primordia, the epidermis of the
siliques and the outer ovule wall, the stigma, petal tips, and floral
nectaries of mature flowers, and the petal/sepal abscission zone of mature
siliques. The presence of GUS activity in guard cells, lateral roots,
pollen grains, leaf vascular tissue, and internal cells of stipules and
nectaries was not confirmed by in situ hybridizations, supporting previous
observations that suggest that the reporter gene is subject to artifactual
expression. These results are consistent with a role for the LTP1 gene
product in some aspect of secretion or deposition of lipophilic substances
in the cell walls of expanding epidermal cells and certain secretory
tissues. The LTP1 promoter region contained sequences homologous to
putative regulatory elements of genes in the phenylpropanoid biosynthetic
pathway, suggesting that the expression of the LTP1 gene may be regulated
by the same or similar mechanisms as genes in the phenylpropanoid pathway.
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