Structure and Expression of an Arabidopsis Acetyl-Coenzyme A Carboxylase Gene
Author(s) -
Keith R. Roesler,
Basil S. Shorrosh,
John B. Ohlrogge
Publication year - 1994
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.105.2.611
Subject(s) - arabidopsis , biology , gene , acetyl coa carboxylase , complementary dna , intron , biochemistry , pyruvate carboxylase , genetics , enzyme , mutant
Acetyl-coenzyme A carboxylase (ACCase) catalyzes the formation of malonyl-coenzyme A, which is used in the plastid for fatty acid synthesis and in the cytosol for several pathways including fatty acid elongation and flavonoid synthesis. Two overlapping Arabidopsis genomic clones were isolated and sequenced to determine the entire ACCase-coding region. Thirty introns with an average size of 94 bp were identified by comparison with an alfalfa ACCase cDNA sequence. The 10-kb Arabidopsis ACCase gene encodes a 251-kD polypeptide, which has 80% amino acid sequence identity with alfalfa ACCase and about 40% identity with ACCase of rat, chicken, yeast, and the diatom Cyclotella. No chloroplast transit peptide sequence was observed, suggesting that this Arabidopsis gene encodes a cytosolic ACCase isozyme. ACCase gene transcripts were detected by RNase protection assays in Arabidopsis root, leaf, silique, and seed. Genomic DNA blot analysis revealed the presence of a second related Arabidopsis ACCase gene.
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