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Plant Physiol, October 2001, Vol. 127, pp. 594-606
Molecular Control of Acid Phosphatase Secretion into the
Rhizosphere of Proteoid Roots from Phosphorus-Stressed White
Lupin1
Susan Stade
Miller,*
Junqi
Liu,
Deborah L.
Allan,
Christopher J.
Menzhuber,
Maria
Fedorova, and
Carroll P.
Vance
Departments of Agronomy and Plant Genetics (S.S.M., J.L., M.F.,
C.P.V.) and Soil, Water and Climate (D.L.A.), University of Minnesota,
St. Paul, Minnesota 55108; University of St. Thomas, St. Paul,
Minnesota 55105 (C.J.M.); and United States Department of Agriculture,
Agricultural Research Service, St. Paul, Minnesota 55108 (C.P.V.)
White lupin (Lupinus albus) grown under P deficiency
displays a suite of highly coordinated adaptive responses. Included
among these is secretion of copious amounts of acid phosphatase
(APase). Although numerous reports document that plants secrete APases in response to P deficiency, little is known of the biochemical and
molecular events involved in this process. Here we characterize the
secreted APase protein, cDNA, and gene from white lupin. The secreted
APase enzyme is a glycoprotein with broad substrate specificity. It is
synthesized as a preprotein with a deduced
Mr of 52,000 containing a 31-amino
acid presequence. Analysis of the presequence predicts that the protein
is targeted to outside the cell. The processed protein has a predicted
Mr of 49,000 but migrates as a protein with
Mr of 70,000 on sodium dodecyl sulfate gels.
This is likely due to glycosylation. Enhanced expression is fairly specific to proteoid roots of P-stressed plants and involves enhanced synthesis of both enzyme protein and mRNA. Secreted APase appears to be
encoded by a single gene containing seven exons interrupted by six
introns. The 5'-upstream putative promoter of the white lupin-secreted
APase contains a 50-base pair region having 72% identity to an
Arabidopsis APase promoter that is responsive to P deficiency. The
white lupin-secreted APase promoter and targeting sequence may be
useful tools for genetically engineering important proteins from plant roots.
1
This work was supported in part by the U.S.
Department of Agriculture-National Research Initiative Competitive
Grants Program (grant no. USDA/98-35100-6098) and by the U.S.
Department of Agriculture-Agricultural Research Service (grant no. CRIS
3640-21000-014-00D). This is a joint contribution of the United
States Department of Agriculture-Agricultural Research Service and the
Minnesota Agricultural Experiment Station Scientific Journal Series.
*
Corresponding author; e-mail mille055{at}tc.umn.edu; fax
651-649-5058.
© 2001 American Society of Plant Physiologists
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