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, Maria F. Drincovich 51Centro de Estudios Fotosinteticos y Bioquimicos, Rosario, Argentina (M.F.D., P.C., C.S.A.) Search for other works by this author on: Oxford Academic Paula Casati 51Centro de Estudios Fotosinteticos y Bioquimicos, Rosario, Argentina (M.F.D., P.C., C.S.A.) Search for other works by this author on: Oxford Academic Carlos S. Andreo 51Centro de Estudios Fotosinteticos y Bioquimicos, Rosario, Argentina (M.F.D., P.C., C.S.A.) Search for other works by this author on: Oxford Academic Saul J. Chessin 52Botany Department, Washington State University, Pullman, Washington 99164–4238 (S.J.C., V.R.F., G.E.E., M.S.B.K.) Search for other works by this author on: Oxford Academic Vincent R. Franceschi 52Botany Department, Washington State University, Pullman, Washington 99164–4238 (S.J.C., V.R.F., G.E.E., M.S.B.K.) Search for other works by this author on: Oxford Academic Gerald E. Edwards 52Botany Department, Washington State University, Pullman, Washington 99164–4238 (S.J.C., V.R.F., G.E.E., M.S.B.K.) Search for other works by this author on: Oxford Academic Maurice S.B. Ku 52Botany Department, Washington State University, Pullman, Washington 99164–4238 (S.J.C., V.R.F., G.E.E., M.S.B.K.) Search for other works by this author on: Oxford Academic
Plant Physiology, Volume 117, Issue 3, July 1998, Pages 733–744, https://doi.org/10.1104/pp.117.3.733
Published:
01 July 1998
Article history
Received:
29 December 1997
Accepted:
06 April 1998
Published:
01 July 1998
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Maria F. Drincovich, Paula Casati, Carlos S. Andreo, Saul J. Chessin, Vincent R. Franceschi, Gerald E. Edwards, Maurice S.B. Ku, Evolution of C4 Photosynthesis inFlaveria Species: Isoforms of NADP-Malic Enzyme, Plant Physiology, Volume 117, Issue 3, July 1998, Pages 733–744, https://doi.org/10.1104/pp.117.3.733
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Abstract
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 ofFlaveria (C3, C3-C4intermediate, 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 C3Flaveria 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 C4species, is localized in bundle-sheath chloroplasts. AmongFlaveria spp. there is a 72-kD constitutive form, a 64-kD form that may have appeared during evolution of C4metabolism, and a 62-kD form that is necessary for the complete functioning of C4 photosynthesis.
Copyright © 1998 American Society of Plant Physiologists
This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)
Issue Section:
BIOCHEMISTRY AND ENZYMOLOGY
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