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Article: The shrimp FAMeT cDNA is encoded for a putative enzyme involved in the methylfarnesoate (MF) biosynthetic pathway and is temporally expressed in the eyestalk of different sexes

TitleThe shrimp FAMeT cDNA is encoded for a putative enzyme involved in the methylfarnesoate (MF) biosynthetic pathway and is temporally expressed in the eyestalk of different sexes
Authors
KeywordsFarnesoic acid O-methyltransferase
Juvenile hormone
Methylfarnesoate
Shrimp
Issue Date2001
PublisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/ibmb
Citation
Insect Biochemistry And Molecular Biology, 2001, v. 31 n. 11, p. 1115-1124 How to Cite?
AbstractMethylfarnesoate (MF), an analogue of the insect juvenile hormone III, has been implicated to play a vital role in the regulation of the growth and reproductive development in crustaceans. Farnesoic acid O-methyltransferase (FAMeT) is the key enzyme involved in catalyzing the final step in the MF biosynthetic pathway. In this study, we report the cloning and characterization of the cDNA encoding the putative FAMeT of the shrimp Metapenaeus ensis. FAMeT comprises 280 amino acid residues with a predicted molecular weight of 32 kDa. The predicted putative FAMeT protein reveals a high degree of structural conservation of FAMeT with the lobsters. It shares 79 and 70% sequence identities with the putative FAMeTs of Homarus americanus and Panulirus interruptus, respectively. As revealed by the Southern blot analysis and genomic PCR, only one gene exists in the shrimp genome and the gene is uninterrupted in the coding region. The shrimp FAMeT mRNA is widely distributed in many tissues with the highest expression level observed in the central nervous system. A constant level of FAMeT expression is recorded in the ventral nerve cord of the juveniles and the mature females during the reproductive cycle. Unlike the ventral nerve cord, the eyestalk of the juvenile male, but not the female, expresses FAMeT. Further study shows that the eyestalk of the mature female expresses FAMeT during all stages of ovarian maturation. We spectulate that FAMeT may be important for the regulation of eyestalk neuropeptides. This is the first extensive study on the molecular characterization, structural analysis and expression of the crustacean FAMeT. © 2001 Elsevier Science Ltd. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/84689
ISSN
2021 Impact Factor: 4.421
2020 SCImago Journal Rankings: 1.718
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSilva Gunawardene, YINen_HK
dc.contributor.authorChow, BKCen_HK
dc.contributor.authorHe, JGen_HK
dc.contributor.authorChan, SMen_HK
dc.date.accessioned2010-09-06T08:55:58Z-
dc.date.available2010-09-06T08:55:58Z-
dc.date.issued2001en_HK
dc.identifier.citationInsect Biochemistry And Molecular Biology, 2001, v. 31 n. 11, p. 1115-1124en_HK
dc.identifier.issn0965-1748en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84689-
dc.description.abstractMethylfarnesoate (MF), an analogue of the insect juvenile hormone III, has been implicated to play a vital role in the regulation of the growth and reproductive development in crustaceans. Farnesoic acid O-methyltransferase (FAMeT) is the key enzyme involved in catalyzing the final step in the MF biosynthetic pathway. In this study, we report the cloning and characterization of the cDNA encoding the putative FAMeT of the shrimp Metapenaeus ensis. FAMeT comprises 280 amino acid residues with a predicted molecular weight of 32 kDa. The predicted putative FAMeT protein reveals a high degree of structural conservation of FAMeT with the lobsters. It shares 79 and 70% sequence identities with the putative FAMeTs of Homarus americanus and Panulirus interruptus, respectively. As revealed by the Southern blot analysis and genomic PCR, only one gene exists in the shrimp genome and the gene is uninterrupted in the coding region. The shrimp FAMeT mRNA is widely distributed in many tissues with the highest expression level observed in the central nervous system. A constant level of FAMeT expression is recorded in the ventral nerve cord of the juveniles and the mature females during the reproductive cycle. Unlike the ventral nerve cord, the eyestalk of the juvenile male, but not the female, expresses FAMeT. Further study shows that the eyestalk of the mature female expresses FAMeT during all stages of ovarian maturation. We spectulate that FAMeT may be important for the regulation of eyestalk neuropeptides. This is the first extensive study on the molecular characterization, structural analysis and expression of the crustacean FAMeT. © 2001 Elsevier Science Ltd. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherPergamon. The Journal's web site is located at http://www.elsevier.com/locate/ibmben_HK
dc.relation.ispartofInsect Biochemistry and Molecular Biologyen_HK
dc.subjectFarnesoic acid O-methyltransferaseen_HK
dc.subjectJuvenile hormoneen_HK
dc.subjectMethylfarnesoateen_HK
dc.subjectShrimpen_HK
dc.titleThe shrimp FAMeT cDNA is encoded for a putative enzyme involved in the methylfarnesoate (MF) biosynthetic pathway and is temporally expressed in the eyestalk of different sexesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0965-1748&volume=31&spage=1115&epage=1124&date=2001&atitle=The+shrimp+FAMeT+cDNA+is+encoded+for+a+putative+enzyme+involved+in+the+methylfarnesoate+(MF)+biosynthetic+pathway+and+is+temporally+expressed+in+the+eyestalk+of+different+sexesen_HK
dc.identifier.emailChow, BKC: bkcc@hku.hken_HK
dc.identifier.authorityChow, BKC=rp00681en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0965-1748(01)00060-1en_HK
dc.identifier.pmid11520690-
dc.identifier.scopuseid_2-s2.0-0034815014en_HK
dc.identifier.hkuros63401en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034815014&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume31en_HK
dc.identifier.issue11en_HK
dc.identifier.spage1115en_HK
dc.identifier.epage1124en_HK
dc.identifier.isiWOS:000171460100009-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridSilva Gunawardene, YIN=6507561163en_HK
dc.identifier.scopusauthoridChow, BKC=7102826193en_HK
dc.identifier.scopusauthoridHe, JG=35487616500en_HK
dc.identifier.scopusauthoridChan, SM=7404255669en_HK
dc.identifier.issnl0965-1748-

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