Isolation of cDNAs from Brassica napus encoding the biotin-binding and transcarboxylase domains of acetyl-CoA carboxylase: assignment of the domain structure in a full-length Arabidopsis thaliana genomic clone.

Elborough, KM; Swinhoe, R; Winz, R; KROON, JTM; Farnsworth, L; Fawcett, T; Martinezrivas, JM; Slabas, AR

Abstract

One independent and two overlapping rape cDNA clones have been isolated from a rape embryo library. We have shown that they encode a 2.3 kb and a 2.5 kb stretch of the full-length acetyl-CoA carboxylase (ACCase) cDNA, corresponding to the biotin-binding and transcarboxylase domains respectively. Using the cDNA in Northern-blot analysis we have shown that the mRNA for ACCase has a higher level of expression in rape seed than in rape leaf and has a full length of 7.5 kb. The level of expression during rape embryogenesis was compared with both oil deposition and expression of two fatty acid synthetase components enoyl-(acyl-carrier-protein) reductase and 3-oxoacyl-(acyl-carrier-protein) reductase. Levels of ACCase mRNA were shown to peak at 29 days after anthesis during embryonic development, similarly to enoyl-(acyl-carrier-protein) reductase and 3-oxoacyl-(acyl-carrier-protein) reductase mRNA. In addition, a full-length genomic clone (19 kb) of Arabidopsis ACCase has been isolated and partially sequenced. Analysis of the clone has allowed the first plant ACCase activity domains (biotin carboxylase-biotin binding-transcarboxylase) to be ordered and assigned. Southern-blot analysis using the Arabidopsis clone indicates that ACCase is a single-copy gene in Arabidopsis but is encoded by a small gene family in rape.

Citation

Elborough, K., Swinhoe, R., Winz, R., KROON, J., Farnsworth, L., Fawcett, T., …Slabas, A. (1994). Isolation of cDNAs from Brassica napus encoding the biotin-binding and transcarboxylase domains of acetyl-CoA carboxylase: assignment of the domain structure in a full-length Arabidopsis thaliana genomic clone. Biochemical Journal, 301(2), 599-605. https://doi.org/10.1042/bj3010599

• Journal Article Type: Article
• Publication Date: Jul 15, 1994
• Journal: Biochemical Journal
• Print ISSN: 0264-6021
• Electronic ISSN: 1470-8728
• Publisher: Portland Press
• Volume: 301
• Issue: 2
• Pages: 599-605
• DOI: https://doi.org/10.1042/bj3010599
• Public URL: https://durham-repository.worktribe.com/output/1557074
• Related Public URLs: http://www.ncbi.nlm.nih.gov/pubmed/7913805