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Plant Physiol, April 2000, Vol. 122, pp. 1057-1072
Coordinate Regulation of the Nuclear and Plastidic Genes Coding
for the Subunits of the Heteromeric Acetyl-Coenzyme A
Carboxylase1
Jinshan
Ke,2
Tuan-Nan
Wen,2
Basil J.
Nikolau, and
Eve Syrkin
Wurtele*
Department of Botany (J.K., E.S.W.) and Department of Biochemistry,
Biophysics, and Molecular Biology (T.-N.W., B.J.N.), Iowa State
University, Ames, Iowa 50011
Plastidic
acetyl-coenzyme A (CoA) carboxylase (ACCase) catalyzes the
first committed reaction of de novo fatty acid biosynthesis. This
heteromeric enzyme is composed of one plastid-coded subunit ( -carboxyltransferase) and three nuclear-coded subunits (biotin carboxy-carrier, biotin carboxylase, and  -carboxyltransferase). We
report the primary structure of the Arabidopsis
-carboxyltransferase and -carboxyltransferase subunits
deduced from nucleotide sequences of the respective genes and/or cDNA.
Co-immunoprecipitation experiments confirm that the
-carboxyltransferase and -carboxyltransferase subunits are
physically associated. The plant -carboxyltransferases have gained a
C-terminal domain relative to eubacteria, possibly via the evolutionary
acquisition of a single exon. This C-terminal domain is
divergent among plants and may have a structural function rather than
being essential for catalysis. The four ACCase subunit mRNAs accumulate
to the highest levels in tissues and cells that are actively
synthesizing fatty acids, which are used either for membrane biogenesis
in rapidly growing tissues or for oil accumulation in developing
embryos. Development coordinately affects changes in the accumulation
of the ACCase subunit mRNAs so that these four mRNAs maintain a
constant molar stoichiometric ratio. These data indicate that the
long-term, developmentally regulated expression of the heteromeric
ACCase is in part controlled by a mechanism(s) that coordinately
affects the steady-state concentrations of each subunit mRNA.
1
This work was supported by the Hatch
Act and State of Iowa funds and by a U.S. Department of
Agriculture-National Research Initiative competitive grant (no.
97-01912 to B.J.N. and E.S.W.), by a grant from the Iowa Soybean
Promotion Board (to E.S.W. and B.J.N.), and by a research award to J.K.
from the Iowa State University Molecular, Cellular, and Developmental
Biology graduate program. This is journal paper no. J-18656 of the
Iowa Agriculture and Home Economics Experiment Station, Ames, project
nos. 2,997 and 2,913.
2
These authors contributed equally to the paper.
*
Corresponding author; e-mail mash{at}iastate.edu; fax
515-294-1337.
© 2000 American Society of Plant Physiologists
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