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PLANT PHYSIOLOGY , Vol 113, Issue 1 75-81, Copyright © 1997 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Targeting of the Arabidopsis Homomeric Acetyl-Coenzyme A Carboxylase to Plastids of Rapeseeds
K. Roesler, D. Shintani, L. Savage, S. Boddupalli and J. Ohlrogge
Department of Botany and Plant Pathology, Michigan State University, East Lansing, Michigan 48824 (K.R., D.S., L.S., J.O.)
Acetyl-coenzyme A carboxylase (ACCase) occurs in at least two forms in
rapeseed (Brassica napus): a homomeric (HO) and presumably cytosolic
isozyme and a heteromeric, plastidial isozyme. We investigated whether the
HO-ACCase of Arabidopsis can be targeted to plastids of B. napus seeds. A
chloroplast transit peptide and the napin promoter were fused to the
Arabidopsis ACC1 gene and transformed into B. napus, with the following
results. (a) The small subunit transit peptide was sufficient to provide
import of this very large protein into developing seed plastids. (b)
HO-ACCase in isolated plastids was found to be biotinylated at a level
comparable to extraplastidial HO-ACCase. (c) In vitro assays of HO-ACCase
in isolated plastids from developing seeds indicate that it occurs as an
enzymatically active form in the plastidial compartment. (d) ACCase
activity in mature B. napus seeds is normally very low; however, plants
expressing the SSU/ACC1 gene had 10- to 20-fold higher ACCase activity in
mature seeds, suggesting that plastid localization prevents the turnover of
HO-ACCase. (e) ACCase over-expression altered seed fatty acid composition,
with the largest effect being an increase in oleic acid. (f) The total oil
content of seeds was increased approximately 5% by the expression of
HO-ACCase in plastids.
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