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

Kuballa, Anna; Guyatt, K. J.; Dixon, Bryony; Thaggard, H.B.; Ashton, Anthony R.; Paterson, B. M.; Merritt, David J.; Elizur, Abigail

doi:10.1016/j.ygcen.2006.07.020

Cited by 40 publications

(29 citation statements)

References 30 publications

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“…Multiple isoforms of FAMeT are common as recently described by Kuballa et al (2007) for crustacean species. Nucleotide analysis of the MsFAMeT isoforms indicated that the second band (or isoform 2) was generated by an excision of a microexon.…”

Section: Discussionmentioning

confidence: 93%

Farnesoic acid O‐methyl transferase (FAMeT) isoforms: Conserved traits and gene expression patterns related to caste differentiation in the stingless bee, Melipona scutellaris

Vieira

Bonetti

Simões

et al. 2007

Arch Insect Biochem Physiol

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Farnesoic acid O-methyl transferase (FAMeT) is the enzyme that catalyzes the formation of methyl farnesoate (MF) from farnesoic acid (FA) in the biosynthetic pathway of juvenile hormone (JH). This work reports the cloning, sequencing, and expression of FAMeT gene from the stingless bee Melipona scutellaris (MsFAMeT). The MsFAMeT in silico analysis showed that greatest sequence similarity is found in Apis mellifera and other insects, while relatively less similarity is shown in crustaceans. Evidence of alternative splicing of a 27 nucleotide (nt) microexon explains the presence of the detected isoforms, 1 and 2. The expression analysis of the two isoforms showed a marked difference when castes were compared, suggesting that they could be involved differently in the JH metabolism in M. scutellaris, providing new insights for the comprehension of female plasticity.

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Section: Discussionmentioning

confidence: 93%

Farnesoic acid O‐methyl transferase (FAMeT) isoforms: Conserved traits and gene expression patterns related to caste differentiation in the stingless bee, Melipona scutellaris

Vieira

Bonetti

Simões

et al. 2007

Arch Insect Biochem Physiol

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“…As reported for M. scutellaris FAMeT, the Ceratitis sequence shows three CK2 phosphorylation sites, suggesting a similar biosynthetic pathway for both genes. Moreover, the long crustacean FAMeT isoform has one CK2 phosphorylation site that is probably involved in the catalytic activity of the enzyme (Kuballa et al, 2007). Like Crustacea and M. scutellaris sequences, the sequence in C. capitata does not show any SAM-binding motif, which would allow S-adenosyl methionine binding in the MF synthesis.…”

Section: Discussionmentioning

confidence: 99%

The putative‐farnesoic acid O‐methyl transferase (FAMeT) gene of Ceratitis capitata: characterization and pre‐imaginal life expression

Vannini

Ciolfi

Spinsanti

et al. 2010

Arch Insect Biochem Physiol

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Farnesoic acid O-methyl transferase (FAMeT) is the enzyme involved in the penultimate step of insect juvenile hormone (JH) biosynthesis and is thus a key regulator in insect development and reproduction. We report the characterization of the putative-FAMeT in the medfly or Mediterranean fruit fly, Ceratitis capitata. This gene was identified by suppressive subtractive hybridization and completely sequenced by the screening of a medfly cDNA library. The obtained sequence was analyzed for conserved protein domain identification and its expression profile was evaluated by quantitative Real-Time PCR in medfly pre-imaginal life. The tissue expression of the isolated gene was verified by in situ hybridization on third instar larvae sections. The characterization of the isolated gene pointed out several typical features of methyl transferase genes. The pre-imaginal putative-FAMeT expression levels were consistent with JH titer change in Diptera. As recognized in some crustaceans, this gene seems to be widely expressed in the medfly as well. Ceratitis capitata is one of the most relevant agricultural pests against which insecticides and the sterile insect technique (SIT) are extensively used in spite of the well-known limitations of these approaches. Although results are not conclusive for the physiological role of the isolated gene, they suggest the characterization of a new gene in the Mediterranean fruit fly potentially involved in JH biosynthesis and may, therefore, have implications for pest control.

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“…In crustaceans, the methyl esterification of FA to MF was thought to be catalyzed by another MTase, farnesoic acid O-methyltransferase (FAMeT), which was well identified in several crustaceans (Gunawardene et al, 2002(Gunawardene et al, , 2001Holford et al, 2004;Hui et al, 2008;Kuballa et al, 2007;Xie et al, 2013;Yang et al, 2012;), FAMeT lacks the signature SAM-binding motif which is present in insects JHAMT, thus it may represent a novel SAM-dependent MTase (Gunawardene et al, 2001). Protein and mRNA of Fig.…”

Section: Introductionmentioning

confidence: 99%

The potential role of juvenile hormone acid methyltransferase in methyl farnesoate (MF) biosynthesis in the swimming crab, Portunus trituberculatus

Xie

Tian

Liu

et al. 2016

Animal Reproduction Science

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Juvenile hormone (JH) and methyl farnesoate (MF) play essential roles in the development and reproduction of insects and crustaceans respectively. Juvenile hormone acid methyltransferase (JHAMT) catalyzes the methyl esterification in insect JH biosynthesis, while the corresponding step in crustacean MF biosynthesis was long thought to be catalyzed by farnesoic acid O-methyltransferase (FAMeT). However, the new discovery of JHAMT orthologs in crustaceans indicates that JHAMT may also play essential role in the MF biosynthesis in crustaceans. Here we cloned and characterized the full-length cDNA encoding JHAMT in the swimming crab Portunus trituberculatus (PtJHAMT). Sequence and structure analysis of PtJHAMT revealed that it was composed of a 6-stranded β sheet with 9 α helices, and contained a signature Sadenosyl-L-methionine (SAM) binding motif, which is the hallmark in all SAM dependent methyltransferases (SAM-MTs). Several active sites that are critical for the interaction of SAM and JH/FA substrate were also conserved in PtJHAMT. The gene expression of PtJHAMT was highly specific to the mandibular organ, which is the sole site of MF synthesis. PtJHAMT expression significantly increased in the late-vitellogenic stage and mature stage, which suggests a possible role of PtJHAMT in modulating ovarian development. The role of PtJHAMT and PtFAMeT in MF biosynthesis was further investigated by RNA interfering (RNAi). Injection of PtJHAMT and PtFAMeT dsRNA both led to a decrease in hemolymph MF titers. Injection of PtHMGR dsRNA caused the decrease in PtJHAMT expression, but had no effect on mRNA level of PtFAMeT. Together these results suggested that JHAMT and FAMeT are both involved in the MF biosynthesis in crustaceans, while the JHAMT is highly specific to FA substrate, and FAMeT may have more catalytic functions.

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

Cited by 40 publications

References 30 publications

Farnesoic acid O‐methyl transferase (FAMeT) isoforms: Conserved traits and gene expression patterns related to caste differentiation in the stingless bee, Melipona scutellaris

Farnesoic acid O‐methyl transferase (FAMeT) isoforms: Conserved traits and gene expression patterns related to caste differentiation in the stingless bee, Melipona scutellaris

The putative‐farnesoic acid O‐methyl transferase (FAMeT) gene of Ceratitis capitata: characterization and pre‐imaginal life expression

The potential role of juvenile hormone acid methyltransferase in methyl farnesoate (MF) biosynthesis in the swimming crab, Portunus trituberculatus

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