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Isolation and expression analysis of multiple isoforms of putative farnesoic acid O-methyltransferase in several crustacean species

Kuballa, A.V. and Guyatt, K. and Dixon, B. and Thaggard, H. and Ashton, A.R. and Paterson, B. and Merritt, D.J. and Elizur, A. (2007) Isolation and expression analysis of multiple isoforms of putative farnesoic acid O-methyltransferase in several crustacean species. General and Comparative Endocrinology, 150 (1). pp. 48-58.

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Article Link(s): http://dx.doi.org/10.1016/j.ygcen.2006.07.020

Publisher URL: http://www.sciencedirect.com

Abstract

Farnesoic acid O-methyltransferase (FaMeT) is the enzyme responsible for the conversion of farnesoic acid (FA) to methyl farnesoate (MF) in the final step of MF synthesis. Multiple isoforms of putative FaMeT were isolated from six crustacean species belonging to the families Portunidae, Penaeidae, Scyllaridae and Parastacidae. The portunid crabs Portunus pelagicus and Scylla serrata code for three forms: short, intermediate and long. Two isoforms (short and long) were isolated from the penaeid prawns Penaeus monodon and Fenneropenaeus merguiensis. Two isoforms were also identified in the scyllarid Thenus orientalis and parastacid Cherax quadricarinatus. Putative FaMeT sequences were also amplified from the genomic DNA of P. pelagicus and compared to the putative FaMeT transcripts expressed. Each putative FaMeT cDNA isoform was represented in the genomic DNA, indicative of a multi-gene family. Various tissues from P. pelagicus were individually screened for putative FaMeT expression using PCR and fragment analysis. Each tissue type expressed all three isoforms of putative FaMeT irrespective of sex or moult stage. Protein domain analysis revealed the presence of a deduced casein kinase II phosphorylation site present only in the long isoform of putative FaMeT.

Item Type:Article
Corporate Creators:Animal Science
Additional Information:© Elsevier Inc.
Keywords:Farnesoic acid O-methyltransferase (FaMeT); methyl farnesoate; multiple isoforms of FaMeT; casein kinase II phosphorylation site; crustacean.
Subjects:Science > Physiology > Animal biochemistry
Aquaculture and Fisheries > Fisheries > Shellfish fisheries
Deposited On:13 Jan 2009 06:11
Last Modified:06 Sep 2010 23:55

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