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J Biol Chem, Vol. 275, Issue 8, 5582-5590, February 25, 2000
From the Departments of The biotin enzyme, 3-methylcrotonyl-CoA
carboxylase (MCCase) (3-methylcrotonyl-CoA:carbon-dioxide ligase
(ADP-forming), EC 6.4.1.4), catalyzes a pivotal reaction required for
both leucine catabolism and isoprenoid metabolism. MCCase is a
heteromeric enzyme composed of biotin-containing (MCC-A) and
non-biotin-containing (MCC-B) subunits. Although the sequence of the
MCC-A subunit was previously determined, the primary structure of the
MCC-B subunit is unknown. Based upon sequences of biotin enzymes that
use substrates structurally related to 3-methylcrotonyl-CoA, we
isolated the MCC-B cDNA and gene of
Arabidopsis. Antibodies directed against the bacterially
produced recombinant protein encoded by the MCC-B cDNA
react solely with the MCC-B subunit of the purified MCCase and inhibit
MCCase activity. The primary structure of the MCC-B subunit shows the
highest similarity to carboxyltransferase domains of biotin enzymes
that use methyl-branched thiol esters as substrate or products. The
single copy MCC-B gene of Arabidopsis is
interrupted by nine introns. MCC-A and MCC-B
mRNAs accumulate in all cell types and organs, with the highest
accumulation occurring in rapidly growing and metabolically active
tissues. In addition, these two mRNAs accumulate coordinately in an
approximately equal molar ratio, and they each account for between 0.01 and 0.1 mol % of cellular mRNA. The sequence of the
Arabidopsis MCC-B gene has enabled the identification of
animal paralogous MCC-B cDNAs and genes, which may have
an impact on the molecular understanding of the lethal inherited
metabolic disorder methylcrotonylglyciuria.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF059510 and AF059511.
Molecular Characterization of the Non-biotin-containing
Subunit of 3-Methylcrotonyl-CoA Carboxylase*
§,,,,, and
Biochemistry, Biophysics, and
Molecular Biology and ¶ Botany, Iowa State University,
Ames, Iowa 50011
*
This work was supported in part by National Science
Foundation Grant IBN-9507549 (to E. S. W. and B. J. N.), a Herman
Frasch award (to E. S. W.), and an Iowa State University Graduate
College research award (to E. S. W.). This is Journal Paper J-18155
of the Iowa Agriculture and Home Economics Experiment Station (Ames, IA), Project Nos. 2997 and 2913; supported by Hatch Act and State of
Iowa funds.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Botany,
441 Bessey Hall, Iowa State University, Ames, IA 50011. Tel.: 515-294-8989; Fax: 515-294-1337; E-mail: mash@iastate.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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