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Molecular cloning, characterization, and elicitation of acetyl-CoA carboxylase from alfalfa

Author:
Shorrosh, B.S., Dixon, R.A., Ohlrogge, J.B.
Source:
Proceedings of the National Academy of Sciences of the United States of America 1994 v.91 no.10 pp. 4323-4327
ISSN:
0027-8424
Subject:
Medicago sativa, complementary DNA, acetyl-CoA carboxylase, nucleotide sequences, amino acid sequences, gene expression, messenger RNA, Colletotrichum lindemuthianum, cell wall components
Abstract:
Acetyl-CoA carboxylase [ACCase; acetyl-CoA:carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] catalyzes the ATP-dependent carboxylation of acetyl CoA to produce malonyl CoA. In plants, malonyl CoA is needed for plastid localized fatty acid biosynthesis and for a variety of pathways in the cytoplasm including flavonoid biosynthesis. We have determined the full nucleotide sequence of an ACCase from alfalfa, which appears to represent a cytoplasmic isozyme. Partial cDNAs were isolated from a cDNA library of suspension culture cells that had been elicited for isoflavonoid phytoalexin synthesis. The full-length sequence was obtained by primer extension and amplification of the cDNA with synthetic primers. The sequence codes for a protein of 2257 amino acids with a calculated Mr of 252,039. The biotin carboxylase, biotin carboxyl carrier protein, and carboxyltransferase domains, respectively, show approximately 72%, 50%, and 65% sequence similarity to those of animal, diatom, and yeast ACCase sequences. ACCase enzyme activity and transcripts are induced severalfold upon addition of yeast or fungal elicitors to alfalfa cell cultures.
Agid:
2355154