Compartmentalization of two forms of acetyl-CoA carboxylase in plants and the origin of their tolerance toward herbicides.

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Abstract
Acetyl-CoA carboxylase (ACCase, EC 6.4.1.2) catalyzes the synthesis of malonyl-CoA, the first intermediate in fatty acid synthesis. We studied the localization of two forms, the prokaryote and the eukaryote forms, of ACCase in pea leaves by comparing the biotin polypeptides of the two ACCases in protein extract from leaves and plastids. We found that the two forms of ACCase were in different cell compartments of pea leaves; the prokaryote form was in the plastids, and the eukaryote form was elsewhere, probably in the cytosol. This result suggested the existence of two sites of malonyl-CoA synthesis. The Gramineae, such as rice and wheat, which lack the accD gene encoding one of the subunits of the prokaryote form of ACCase in their chloroplast genomes, did not have the prokaryote form of the enzyme but had the eukaryote form. The selective grass herbicides of the diphenoxypropionic acid type and the cyclohexanedione type, in vitro, inhibited plastidic ACCase of the eukaryote form from wheat but did not inhibit that of the prokaryote form from pea, suggesting that the origin of the tolerance of intact pea plant toward these herbicides is partly in the insensitivity of the prokaryote form of the enzyme. The origin of the susceptibility of the Gramineae plants toward these herbicides seems to lie in the presence of the herbicide-sensitive eukaryote form and the absence of the insensitive prokaryote form due to the lack of the accD gene in plastid.