KM Elborough
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
Authors
R Swinhoe
R Winz
Dr Johannes Kroon j.t.m.kroon@durham.ac.uk
Senior Experimental Officer
L Farnsworth
Professor Tony Fawcett tony.fawcett@durham.ac.uk
Pro Vice-Chancellor (Education)
JM Martinezrivas
AR Slabas
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 |
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