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A farnesoic acid O-methyltransferase (FAMeT) from Exopalaemon carinicauda is responsive to Vibrio anguillarum and WSSV challenge

Methyl farnesoate (MF), an analogue of the insect juvenile hormone III, is believed to play important roles in the regulation of the growth and reproductive development in crustaceans. Farnesoic acid O-methyltransferase (FAMeT) is the key enzyme in the juvenile hormone biosynthetic pathway, involved...

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Autores principales: Duan, Yafei, Liu, Ping, Li, Jitao, Wang, Yun, Li, Jian, Chen, Ping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3982035/
https://www.ncbi.nlm.nih.gov/pubmed/24136172
http://dx.doi.org/10.1007/s12192-013-0464-5
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author Duan, Yafei
Liu, Ping
Li, Jitao
Wang, Yun
Li, Jian
Chen, Ping
author_facet Duan, Yafei
Liu, Ping
Li, Jitao
Wang, Yun
Li, Jian
Chen, Ping
author_sort Duan, Yafei
collection PubMed
description Methyl farnesoate (MF), an analogue of the insect juvenile hormone III, is believed to play important roles in the regulation of the growth and reproductive development in crustaceans. Farnesoic acid O-methyltransferase (FAMeT) is the key enzyme in the juvenile hormone biosynthetic pathway, involved in the conversion of farnesoic acid (FA) to MF in the final step of MF synthesis. In this study, a FAMeT cDNA (named EcFAMeT) was cloned from the hemocytes of ridgetail white prawn Exopalaemon carinicauda by rapid amplification of cDNA ends (RACE) methods. The full-length cDNA of EcFAMeT was 1,620 bp, including contains a 5′-untranslated region (UTR) of 75 bp, 3′-UTR of 714 bp with a poly (A) tail, an open reading frame (ORF) of 831 bp, encoding a 276-amino-acid polypeptide with the predicted molecular weight of 31.57 kDa and estimated isoelectric point of 4.67. BLAST analysis revealed that amino acids of EcFAMeT shared high identity (75–90 %) with that of other crustaceans. Two conserved signatures domains of Methyltransf-FA superfamily were also identified in EcFAMeT. Real time quantitative RT-PCR analysis indicated that EcFAMeT could be detected in all the tested tissues and strongly expressed in hepatopancreas and ovary of E. carinicauda. After Vibrio anguillarum and WSSV challenge, EcFAMeT transcripts both in hemocytes and hepatopancreas increased significantly in the first 3 h, respectively. The results indicated that EcFAMeT might be associated with the immune defenses to V. anguillarum and WSSV in E. carinicauda.
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spelling pubmed-39820352014-04-23 A farnesoic acid O-methyltransferase (FAMeT) from Exopalaemon carinicauda is responsive to Vibrio anguillarum and WSSV challenge Duan, Yafei Liu, Ping Li, Jitao Wang, Yun Li, Jian Chen, Ping Cell Stress Chaperones Original Paper Methyl farnesoate (MF), an analogue of the insect juvenile hormone III, is believed to play important roles in the regulation of the growth and reproductive development in crustaceans. Farnesoic acid O-methyltransferase (FAMeT) is the key enzyme in the juvenile hormone biosynthetic pathway, involved in the conversion of farnesoic acid (FA) to MF in the final step of MF synthesis. In this study, a FAMeT cDNA (named EcFAMeT) was cloned from the hemocytes of ridgetail white prawn Exopalaemon carinicauda by rapid amplification of cDNA ends (RACE) methods. The full-length cDNA of EcFAMeT was 1,620 bp, including contains a 5′-untranslated region (UTR) of 75 bp, 3′-UTR of 714 bp with a poly (A) tail, an open reading frame (ORF) of 831 bp, encoding a 276-amino-acid polypeptide with the predicted molecular weight of 31.57 kDa and estimated isoelectric point of 4.67. BLAST analysis revealed that amino acids of EcFAMeT shared high identity (75–90 %) with that of other crustaceans. Two conserved signatures domains of Methyltransf-FA superfamily were also identified in EcFAMeT. Real time quantitative RT-PCR analysis indicated that EcFAMeT could be detected in all the tested tissues and strongly expressed in hepatopancreas and ovary of E. carinicauda. After Vibrio anguillarum and WSSV challenge, EcFAMeT transcripts both in hemocytes and hepatopancreas increased significantly in the first 3 h, respectively. The results indicated that EcFAMeT might be associated with the immune defenses to V. anguillarum and WSSV in E. carinicauda. Springer Netherlands 2013-10-19 2014-05 /pmc/articles/PMC3982035/ /pubmed/24136172 http://dx.doi.org/10.1007/s12192-013-0464-5 Text en © The Author(s) 2013 https://creativecommons.org/licenses/by-nc/2.0/ Open Access This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Original Paper
Duan, Yafei
Liu, Ping
Li, Jitao
Wang, Yun
Li, Jian
Chen, Ping
A farnesoic acid O-methyltransferase (FAMeT) from Exopalaemon carinicauda is responsive to Vibrio anguillarum and WSSV challenge
title A farnesoic acid O-methyltransferase (FAMeT) from Exopalaemon carinicauda is responsive to Vibrio anguillarum and WSSV challenge
title_full A farnesoic acid O-methyltransferase (FAMeT) from Exopalaemon carinicauda is responsive to Vibrio anguillarum and WSSV challenge
title_fullStr A farnesoic acid O-methyltransferase (FAMeT) from Exopalaemon carinicauda is responsive to Vibrio anguillarum and WSSV challenge
title_full_unstemmed A farnesoic acid O-methyltransferase (FAMeT) from Exopalaemon carinicauda is responsive to Vibrio anguillarum and WSSV challenge
title_short A farnesoic acid O-methyltransferase (FAMeT) from Exopalaemon carinicauda is responsive to Vibrio anguillarum and WSSV challenge
title_sort farnesoic acid o-methyltransferase (famet) from exopalaemon carinicauda is responsive to vibrio anguillarum and wssv challenge
topic Original Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3982035/
https://www.ncbi.nlm.nih.gov/pubmed/24136172
http://dx.doi.org/10.1007/s12192-013-0464-5
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