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Molecular characterization of a novel, nuclear-encoded, NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase in plastids of the gymnosperm Pinus sylvestris L.

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Abstract

Angiosperms and algae possess two distinct glyceraldehyde-3-phosphate dehydrogenase (GAPDH) enzymes, an NAD+-dependent tetramer involved in cytosolic glycolysis and an NADP+-dependent enzyme of the Calvin cycle in chloroplasts. We have found that the gymnosperm Pinus sylvestris possesses, in addition to these, a nuclear-encoded, plastid-specific, NAD+-dependent GAPDH, designated GapCp, which has not previously been described from any plant. Several independent full-size cDNAs for this enzyme were isolated which encode a functional transit peptide and mature subunit very similar to that of cytosolic GAPDH of angiosperms and algae. A molecular phylogeny reveals that chloroplast GapCp and cytosolic GapC arose through gene duplication early in chlorophyte evolution. The GapCp gene is expressed as highly as that for GapC in light-grown pine seedlings. These findings suggest that aspects of compartmentalized sugar phosphate metabolism may differ in angiosperms and gymnosperms and furthermore underscore the contributions of endosymbiotic gene transfer and gene duplication to the nuclear complement of genes for enzymes of plant primary metabolism.

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Authors and Affiliations

  1. Institut für Genetik, Technische Universität Braunschweig, Spielmannstrasse 7, D-38023, Braunschweig, FRG

    Gilbert Meyer-Gauen, Rüdiger Cerff & William Martin

  2. Institut für Pflanzenphysiologie und Mikrobiologie, Freie Universität Berlin, Königin-Luise-Strasse 12-16a, D-14195, Berlin, FRG

    Claus Schnarrenberger

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  1. Gilbert Meyer-Gauen
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Meyer-Gauen, G., Schnarrenberger, C., Cerff, R. et al. Molecular characterization of a novel, nuclear-encoded, NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase in plastids of the gymnosperm Pinus sylvestris L.. Plant Mol Biol 26, 1155–1166 (1994). https://doi.org/10.1007/BF00040696

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