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Evolution of C4 Photosynthesis in Flaveria Species1
Isoforms of NADP-Malic Enzyme

Maria F. Drincovich, Paula Casati, Carlos S. Andreo, Saul J. Chessin, Vincent R. Franceschi, Gerald E. Edwards*, and Maurice S.B. Ku

Centro de Estudios Fotosinteticos y Bioquimicos, Rosario, Argentina (M.F.D., P.C., C.S.A.); and Botany Department, Washington State University, Pullman, Washington 99164-4238 (S.J.C., V.R.F., G.E.E., M.S.B.K.)

NADP-malic enzyme (NADP-ME, EC 1.1.1.40), a key enzyme in C4 photosynthesis, provides CO2 to the bundle-sheath chloroplasts, where it is fixed by ribulose-1,5-bisphosphate carboxylase/oxygenase. We characterized the isoform pattern of NADP-ME in different photosynthetic species of Flaveria (C3, C3-C4 intermediate, C4-like, C4) based on sucrose density gradient centrifugation and isoelectric focusing of the native protein, western-blot analysis of the denatured protein, and in situ immunolocalization with antibody against the 62-kD C4 isoform of maize. A 72-kD isoform, present to varying degrees in all species examined, is predominant in leaves of C3 Flaveria spp. and is also present in stem and root tissue. By immunolabeling, NADP-ME was found to be mostly localized in the upper palisade mesophyll chloroplasts of C3 photosynthetic tissue. Two other isoforms of the enzyme, with molecular masses of 62 and 64 kD, occur in leaves of certain intermediates having C4 cycle activity. The 62-kD isoform, which is the predominant highly active form in the C4 species, is localized in bundle-sheath chloroplasts. Among Flaveria spp. there is a 72-kD constitutive form, a 64-kD form that may have appeared during evolution of C4 metabolism, and a 62-kD form that is necessary for the complete functioning of C4 photosynthesis.

1   This research was supported by the National Science Foundation (grant no. IBN 93-17756 to G.E.E.) and by grants from the Consejo Nacional de Investigaciones Científicas y Técnicas and Fundación Antorchas (to C.S.A.).
*   Corresponding author; e-mail edwardsg{at}wsu.edu; fax 1-509-335-3517.

Plant Physiol. (1998) 117: 733-744
Copyright Clearance Center:   0032-0889/98/117/0733/12
© 1998 American Society of Plant Physiologists




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