Molecular and functional characterization of a juvenile hormone acid methyltransferase expressed in the corpora allata of mosquitoes
A juvenile hormone acid methyltransferase (JHAMT) was isolated as an abundant EST in a library of the corpora allata of the adult female mosquito Aedes aegypti. Its full length cDNA encodes a 278-aa protein that has 43% amino acid identity with BmJHAMT, a juvenile hormone acid methyltransferase prev...
Guardado en:
| Publicado: |
2009
|
|---|---|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09651748_v39_n1_p31_Mayoral http://hdl.handle.net/20.500.12110/paper_09651748_v39_n1_p31_Mayoral |
| Aporte de: |
| id |
paper:paper_09651748_v39_n1_p31_Mayoral |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_09651748_v39_n1_p31_Mayoral2023-06-08T15:58:38Z Molecular and functional characterization of a juvenile hormone acid methyltransferase expressed in the corpora allata of mosquitoes Aedes aegypti Farnesoic acid Juvenile hormone Methyltransferase Mosquito insect protein juvenile hormone methyltransferase amino acid sequence animal article chemistry corpus allatum enzymology female gene expression genetics growth, development and aging metabolism molecular cloning molecular genetics mosquito sequence alignment Amino Acid Sequence Animals Cloning, Molecular Corpora Allata Culicidae Female Gene Expression Insect Proteins Juvenile Hormones Methyltransferases Molecular Sequence Data Sequence Alignment Aedes aegypti Bombyx mori A juvenile hormone acid methyltransferase (JHAMT) was isolated as an abundant EST in a library of the corpora allata of the adult female mosquito Aedes aegypti. Its full length cDNA encodes a 278-aa protein that has 43% amino acid identity with BmJHAMT, a juvenile hormone acid methyltransferase previously cloned from Bombyx mori. Heterologous expression produced a recombinant protein that metabolizes farnesoic acid (FA) into methyl farnesoate, as well as juvenile hormone acid into juvenile hormone III (JH III) with exquisite stereo specificity. Real time PCR experiments showed that JHAMT mRNA levels are not an unequivocal indicator of JH III synthesis rates; the A. aegypti JHAMT gene, silent in female pupae, was transcriptionally activated just 4-6 h before adult eclosion. Radiochemical methyltransferase assays using active and inactive corpora allata glands (CA) dissected from sugar and blood-fed females respectively, clearly indicated that significant levels of JHAMT enzymatic activity are present when the CA shows very low spontaneous rates of JH III synthesis. Having the last enzymes of the JH synthetic pathway readily available all the time might be critical for the adult female mosquito to sustain rapid dynamic changes in JH III synthesis in response to nutritional changes or peripheral influences, such as mating or feeding. These results suggest that this gene has different roles in the regulation of JH synthesis in pupal and adult female mosquitoes, and support the hypothesis that the rate-limiting steps in JH III synthesis in adult female mosquitoes are located before entrance of FA into the synthetic pathway. 2009 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09651748_v39_n1_p31_Mayoral http://hdl.handle.net/20.500.12110/paper_09651748_v39_n1_p31_Mayoral |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Aedes aegypti Farnesoic acid Juvenile hormone Methyltransferase Mosquito insect protein juvenile hormone methyltransferase amino acid sequence animal article chemistry corpus allatum enzymology female gene expression genetics growth, development and aging metabolism molecular cloning molecular genetics mosquito sequence alignment Amino Acid Sequence Animals Cloning, Molecular Corpora Allata Culicidae Female Gene Expression Insect Proteins Juvenile Hormones Methyltransferases Molecular Sequence Data Sequence Alignment Aedes aegypti Bombyx mori |
| spellingShingle |
Aedes aegypti Farnesoic acid Juvenile hormone Methyltransferase Mosquito insect protein juvenile hormone methyltransferase amino acid sequence animal article chemistry corpus allatum enzymology female gene expression genetics growth, development and aging metabolism molecular cloning molecular genetics mosquito sequence alignment Amino Acid Sequence Animals Cloning, Molecular Corpora Allata Culicidae Female Gene Expression Insect Proteins Juvenile Hormones Methyltransferases Molecular Sequence Data Sequence Alignment Aedes aegypti Bombyx mori Molecular and functional characterization of a juvenile hormone acid methyltransferase expressed in the corpora allata of mosquitoes |
| topic_facet |
Aedes aegypti Farnesoic acid Juvenile hormone Methyltransferase Mosquito insect protein juvenile hormone methyltransferase amino acid sequence animal article chemistry corpus allatum enzymology female gene expression genetics growth, development and aging metabolism molecular cloning molecular genetics mosquito sequence alignment Amino Acid Sequence Animals Cloning, Molecular Corpora Allata Culicidae Female Gene Expression Insect Proteins Juvenile Hormones Methyltransferases Molecular Sequence Data Sequence Alignment Aedes aegypti Bombyx mori |
| description |
A juvenile hormone acid methyltransferase (JHAMT) was isolated as an abundant EST in a library of the corpora allata of the adult female mosquito Aedes aegypti. Its full length cDNA encodes a 278-aa protein that has 43% amino acid identity with BmJHAMT, a juvenile hormone acid methyltransferase previously cloned from Bombyx mori. Heterologous expression produced a recombinant protein that metabolizes farnesoic acid (FA) into methyl farnesoate, as well as juvenile hormone acid into juvenile hormone III (JH III) with exquisite stereo specificity. Real time PCR experiments showed that JHAMT mRNA levels are not an unequivocal indicator of JH III synthesis rates; the A. aegypti JHAMT gene, silent in female pupae, was transcriptionally activated just 4-6 h before adult eclosion. Radiochemical methyltransferase assays using active and inactive corpora allata glands (CA) dissected from sugar and blood-fed females respectively, clearly indicated that significant levels of JHAMT enzymatic activity are present when the CA shows very low spontaneous rates of JH III synthesis. Having the last enzymes of the JH synthetic pathway readily available all the time might be critical for the adult female mosquito to sustain rapid dynamic changes in JH III synthesis in response to nutritional changes or peripheral influences, such as mating or feeding. These results suggest that this gene has different roles in the regulation of JH synthesis in pupal and adult female mosquitoes, and support the hypothesis that the rate-limiting steps in JH III synthesis in adult female mosquitoes are located before entrance of FA into the synthetic pathway. |
| title |
Molecular and functional characterization of a juvenile hormone acid methyltransferase expressed in the corpora allata of mosquitoes |
| title_short |
Molecular and functional characterization of a juvenile hormone acid methyltransferase expressed in the corpora allata of mosquitoes |
| title_full |
Molecular and functional characterization of a juvenile hormone acid methyltransferase expressed in the corpora allata of mosquitoes |
| title_fullStr |
Molecular and functional characterization of a juvenile hormone acid methyltransferase expressed in the corpora allata of mosquitoes |
| title_full_unstemmed |
Molecular and functional characterization of a juvenile hormone acid methyltransferase expressed in the corpora allata of mosquitoes |
| title_sort |
molecular and functional characterization of a juvenile hormone acid methyltransferase expressed in the corpora allata of mosquitoes |
| publishDate |
2009 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09651748_v39_n1_p31_Mayoral http://hdl.handle.net/20.500.12110/paper_09651748_v39_n1_p31_Mayoral |
| _version_ |
1768546310990856192 |