MOLECULAR CHARACTERIZATION OF A NOVEL, NUCLEAR-ENCODED, NAD(-DEPENDENT GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE IN PLASTIDS OF THE GYMNOSPERM PINUS-SYLVESTRIS L())
G. Meyergauen et al., MOLECULAR CHARACTERIZATION OF A NOVEL, NUCLEAR-ENCODED, NAD(-DEPENDENT GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE IN PLASTIDS OF THE GYMNOSPERM PINUS-SYLVESTRIS L()), Plant molecular biology, 26(4), 1994, pp. 1155-1166
Angiosperms and algae possess two distinct glyceraldehyde-3-phosphate
dehydrogenase (GAPDH) enzymes, an NAD(+)-dependent tetramer involved i
n cytosolic glycolysis and an NADP(+)-dependent enzyme of the Calvin c
ycle in chloroplasts. We have found that the gymnosperm Pinus sylvestr
is possesses, in addition to these, a nuclear-encoded, plastid-specifi
c, 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 a
nd mature subunit very similar to that of cytosolic GAPDH of angiosper
ms and algae. A molecular phylogeny reveals that chloroplast GapCp and
cytosolic GapC arose through gene duplication early in chlorophyte ev
olution. The GapCp gene is expressed as highly as that for GapC in lig
ht-grown pine seedlings. These findings suggest that aspects of compar
tmentalized sugar phosphate metabolism may differ in angiosperms and g
ymnosperms and furthermore underscore the contributions of endosymbiot
ic gene transfer and gene duplication to the nuclear complement of gen
es for enzymes of plant primary metabolism.