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Osmotic Stress Induces Expression of Choline Monooxygenase in
Sugar Beet and Amaranth1
Brenda L. Russell,
Bala Rathinasabapathi, and
Andrew D. Hanson*
Horticultural Sciences Department, University of Florida,
Gainesville, Florida 32611
Choline monooxygenase (CMO) catalyzes
the committing step in the synthesis of glycine betaine, an
osmoprotectant accumulated by many plants in response to salinity and
drought. To investigate how these stresses affect CMO expression, a
spinach (Spinacia oleracea L., Chenopodiaceae) probe was
used to isolate CMO cDNAs from sugar beet (Beta vulgaris
L., Chenopodiaceae), a salt- and drought-tolerant crop. The deduced
beet CMO amino acid sequence comprised a transit peptide and a
381-residue mature peptide that was 84% identical (97% similar) to
that of spinach and that showed the same consensus motif for
coordinating a Rieske-type [2Fe-2S] cluster. A mononuclear Fe-binding
motif was also present. When water was withheld, leaf relative water
content declined to 59% and the levels of CMO mRNA, protein, and
enzyme activity rose 3- to 5-fold; rewatering reversed these changes.
After gradual salinization (NaCl:CaCl2 = 5.7:1, mol/mol),
CMO mRNA, protein, and enzyme levels in leaves increased 3- to 7-fold
at 400 mm salt, and returned to uninduced levels when salt
was removed. Beet roots also expressed CMO, most strongly when
salinized. Salt-inducible CMO mRNA, protein, and enzyme activity were
readily detected in leaves of Amaranthus caudatus L. (Amaranthaceae). These data show that CMO most probably has a
mononuclear Fe center, is inducibly expressed in roots as well as in
leaves of Chenopodiaceae, and is not unique to this family.
1
This work was supported in part by a grant from
the U.S. Department of Agriculture National Research Initiative
Competitive Grants Program (95-37100-1596) and by an endowment from the
C.V. Griffin, Sr. Foundation. This is Florida Agricultural Experiment Station journal series no. R-06188.
*
Corresponding author; e-mail adha{at}gnv.ifas.ufl.edu; fax
1-352-392-6479.
Plant Physiol. (1998) 116: 859-865
Copyright Clearance Center: 0032-0889/98/116/0859/07
© 1998 American Society of Plant Physiologists
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