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

Anna V Kuballa; K Guyatt; B Dixon; H Thaggard; A R Ashton; B Paterson; D J Merritt; Abigail Elizur

doi:10.1016/j.ygcen.2006.07.020

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

Journal article

Peer reviewed

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

Anna V Kuballa, K Guyatt, B Dixon, H Thaggard, A R Ashton, B Paterson, D J Merritt and Abigail Elizur

General and Comparative Endocrinology, Vol.150(1), pp.48-58

2007

DOI: https://doi.org/10.1016/j.ygcen.2006.07.020

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Abstract

farnesoic acid O-methyltransferase (FaMeT)

methyl farnesoate

multiple isoforms of FaMeT

casein kinase II phosphorylation site

crustaceans

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.

Details

Title: Isolation and expression analysis of multiple isoforms of putative farnesoic acid O-methyltransferase in several crustacean species
Authors: Anna V Kuballa (Author) - Queensland Department of Primary Industries & Fisheries
K Guyatt (Author) - Queensland Department of Primary Industries & Fisheries
B Dixon (Author) - Queensland Department of Primary Industries & Fisheries
H Thaggard (Author) - Queensland Department of Primary Industries & Fisheries
A R Ashton (Author) - CSIRO Plant Industry
B Paterson (Author) - Queensland Department of Primary Industries & Fisheries
D J Merritt (Author) - University of Queensland
Abigail Elizur (Author) - University of the Sunshine Coast - Faculty of Science, Health and Education
Publication details: General and Comparative Endocrinology, Vol.150(1), pp.48-58
Publisher: Academic Press
Date published: 2007
DOI: 10.1016/j.ygcen.2006.07.020
ISSN: 0016-6480
Organisation Unit: School of Health - Biomedicine; University of the Sunshine Coast, Queensland; School of Health and Sport Sciences - Legacy; Centre for Bioinnovation; School of Health and Behavioural Sciences - Legacy
Language: English
Record Identifier: 99449911602621
Output Type: Journal article

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Collaboration types: Domestic collaboration
Web Of Science research areas: Endocrinology & Metabolism; Zoology

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