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A novel composite locus of Arabidopsis encoding two polypeptides with metabolically related but distinct functions in lysine catabolism
Author(s) -
Tang Guiliang,
Zhu Xiaohong,
Tang Xiaohu,
Galili Gad
Publication year - 2000
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.2000.00770.x
Subject(s) - arabidopsis , biology , lysine , phosphofructokinase 2 , gene , catabolism , biochemistry , locus (genetics) , genetics , mutant , enzyme , amino acid
Summary Both plants and animals catabolise lysine via saccharopine by two consecutive enzymes, lysine‐ketoglutarate reductase (LKR) and saccharopine dehydrogenase (SDH), which are linked on a single polypeptide. We recently demonstrated that Arabidopsis plants possess not only a bifunctional LKR/SDH but in addition a monofunctional SDH enzyme. We also speculated that these two enzymes may be controlled by a single gene (G. Tang et al . Plant Cell , 1997, 9, 1305–1316). By expressing several epitope‐tagged and GUS reporter constructs, we demonstrate in the present study that the Arabidopsis monofunctional SDH is encoded by a distinct gene, which is, however, nested entirely within the coding and 3′ non‐coding regions of the larger bifunctional LKR/SDH gene. The entire open reading frame of the monofunctional SDH gene, as well as some components of its promoter, are also parts of the translated coding sequence of the bifunctional LKR/SDH gene. These special structural characteristics, combined with the fact that the two genes encode simultaneously two metabolically related but distinct enzymes, render the LKR/SDH locus a novel type of a composite locus. Not all plant species possess an active monofunctional SDH gene and the production of this enzyme is correlated with an increased flux of lysine catabolism. Taken together, our results suggest that the composite LKR/SDH locus serves to control an efficient, highly regulated flux of lysine catabolism