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Plant Physiol, January 2002, Vol. 128, pp. 125-139
Distinct But Conserved Functions for Two Chloroplastic NADP-Malic
Enzyme Isoforms in C3 and
C4 Flaveria Species1
Lien B.
Lai,2
Lin
Wang,3 and
Timothy M.
Nelson*
Department of Molecular, Cellular and Developmental Biology, Yale
University, New Haven, Connecticut 06520-8104
In the most common C4 pathway for carbon
fixation, an NADP-malic enzyme (NADP-ME) decarboxylates malate in the
chloroplasts of bundle sheath cells. Isoforms of plastidic NADP-ME are
encoded by two genes in all species of Flaveria,
including C3, C3-C4 intermediate, and C4 types. However, only one of these genes,
ChlMe1, encodes the enzyme that functions in the
C4 pathway. We compared the expression patterns of the
ChlMe1 and ChlMe2 genes in developing
leaves of Flaveria pringlei (C3) and
Flaveria trinervia (C4) and in transgenic Flaveria bidentis (C4).
ChlMe1 expression in C4 species increases in
leaves with high C4 pathway activity. In the C3
species F. pringlei, ChlMe1 expression is
transient and limited to early leaf development. In contrast,
ChlMe2 is expressed in C3 and C4 species concurrent with stages in chloroplast biogenesis. Because previous studies suggest that NADP-ME activities generally reflect the
level of its mRNA abundance, we discuss possible roles of ChlMe1 and ChlMe2 based on these
expression patterns.
1
This work was supported by the Department of
Energy (grant no. DE-FG02-91ER20038).
2
Present address: Department of Plant Biology, The Ohio
State University, Columbus, OH 43210-1293.
3
Present address: Yale University, Department of
Laboratory Medicine, New Haven, CT 06520-8035.
*
Corresponding author; e-mail timothy.nelson{at}yale.edu; fax
203-432-5632.
© 2002 American Society of Plant Physiologists
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