File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1016/S0965-1748(01)00060-1
- Scopus: eid_2-s2.0-0034815014
- PMID: 11520690
- WOS: WOS:000171460100009
- Find via
Supplementary
- Citations:
- Appears in Collections:
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
Title | 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 |
---|---|
Authors | |
Keywords | Farnesoic acid O-methyltransferase Juvenile hormone Methylfarnesoate Shrimp |
Issue Date | 2001 |
Publisher | Pergamon. 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? |
Abstract | Methylfarnesoate (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 Identifier | http://hdl.handle.net/10722/84689 |
ISSN | 2023 Impact Factor: 3.2 2023 SCImago Journal Rankings: 0.909 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Silva Gunawardene, YIN | en_HK |
dc.contributor.author | Chow, BKC | en_HK |
dc.contributor.author | He, JG | en_HK |
dc.contributor.author | Chan, SM | en_HK |
dc.date.accessioned | 2010-09-06T08:55:58Z | - |
dc.date.available | 2010-09-06T08:55:58Z | - |
dc.date.issued | 2001 | en_HK |
dc.identifier.citation | Insect Biochemistry And Molecular Biology, 2001, v. 31 n. 11, p. 1115-1124 | en_HK |
dc.identifier.issn | 0965-1748 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/84689 | - |
dc.description.abstract | Methylfarnesoate (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.language | eng | en_HK |
dc.publisher | Pergamon. The Journal's web site is located at http://www.elsevier.com/locate/ibmb | en_HK |
dc.relation.ispartof | Insect Biochemistry and Molecular Biology | en_HK |
dc.subject | Farnesoic acid O-methyltransferase | en_HK |
dc.subject | Juvenile hormone | en_HK |
dc.subject | Methylfarnesoate | en_HK |
dc.subject | Shrimp | en_HK |
dc.title | 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 | en_HK |
dc.type | Article | en_HK |
dc.identifier.openurl | http://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+sexes | en_HK |
dc.identifier.email | Chow, BKC: bkcc@hku.hk | en_HK |
dc.identifier.authority | Chow, BKC=rp00681 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/S0965-1748(01)00060-1 | en_HK |
dc.identifier.pmid | 11520690 | - |
dc.identifier.scopus | eid_2-s2.0-0034815014 | en_HK |
dc.identifier.hkuros | 63401 | en_HK |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0034815014&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 31 | en_HK |
dc.identifier.issue | 11 | en_HK |
dc.identifier.spage | 1115 | en_HK |
dc.identifier.epage | 1124 | en_HK |
dc.identifier.isi | WOS:000171460100009 | - |
dc.publisher.place | United Kingdom | en_HK |
dc.identifier.scopusauthorid | Silva Gunawardene, YIN=6507561163 | en_HK |
dc.identifier.scopusauthorid | Chow, BKC=7102826193 | en_HK |
dc.identifier.scopusauthorid | He, JG=35487616500 | en_HK |
dc.identifier.scopusauthorid | Chan, SM=7404255669 | en_HK |
dc.identifier.issnl | 0965-1748 | - |