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קהילה:
אסיף מאגר המחקר החקלאי
פותח על ידי קלירמאש פתרונות בע"מ -
Pheromone biosynthetic pathways: PBAN-regulated rate-limiting steps and differential expression of desaturase genes in moth species
Year:
2008
Authors :
זאדה (לוי), ענת
;
.
עזריאלי, אבי
;
.
פלח, לילי
;
.
צפדיה, אורן
;
.
רפאלי, עדה
;
.
Volume :
38
Co-Authors:
Tsfadia, O., Institute for Technology and Storage of Agricultural Products, ARO, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Azrielli, A., Institute for Technology and Storage of Agricultural Products, ARO, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Falach, L., Institute of Plant Protection, Agriculture Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Zada, A., Institute of Plant Protection, Agriculture Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Roelofs, W., Department of Entomology, Cornell University, Geneva, NY 11456, United States
Rafaeli, A., Institute for Technology and Storage of Agricultural Products, ARO, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Facilitators :
From page:
552
To page:
567
(
Total pages:
16
)
Abstract:
We combine the use of labeled precursors with enzyme inhibitors to decipher the biosynthetic pathway of pheromone biosynthesis and the rate-limiting step/s that are regulated by pheromone biosynthesis activating neuropeptide (PBAN). We demonstrate that Plodia interpunctella is able to utilize hexadecanoic acid, and to a lesser extent tetradecanoic acid, for the biosynthesis of the main pheromone component (Z,E)-9,12-tetradecadienyl acetate. This indicated that the main pathway involves a Δ11 desaturase, chain shortening, followed by a Δ12 desaturase, but that a functional Δ9 desaturase could also be utilized. Using reverse transcription-quantitative real-time polymerase chain reaction (RT-QPCR) we distinguish two out of nine possible desaturase gene transcripts in P. interpunctella that are expressed at the highest levels. The rate-limiting step for PBAN-stimulation was studied in two moth species so as to compare the biosynthesis of a diene (P. interpunctella) and a monoene (Helicoverpa armigera) main pheromone component. In both species, incorporation of label from the 13C sodium acetate precursor was activated by PBAN whereas no stimulatory action was observed in the incorporation of the precursors: 13C malonyl coenzyme A; hexadecanoic 16,16,16-2H3 or tetradecanoic 14,14,14-2H3 acids. The acetyl coenzyme A carboxylase (ACCase) inhibitor, Tralkoxydim, inhibited the PBAN-stimulation of incorporation of stable isotope whereas the fatty-acyl reductase inhibitor, Mevastatin, failed to influence the stimulatory action of PBAN. These results provide irrefutable support to the hypothesis that PBAN affects the production of malonyl coenzyme A from acetate by the action of ACCase in the pheromone glands of these moths. © 2008 Elsevier Ltd. All rights reserved.
Note:
Related Files :
Animals
biosynthesis
Female
gene expression
Genetics
Lepidoptera
Male
pheromones
sexual development
עוד תגיות
תוכן קשור
More details
DOI :
10.1016/j.ibmb.2008.01.005
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
31768
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 01:05
You may also be interested in
Scientific Publication
Pheromone biosynthetic pathways: PBAN-regulated rate-limiting steps and differential expression of desaturase genes in moth species
38
Tsfadia, O., Institute for Technology and Storage of Agricultural Products, ARO, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Azrielli, A., Institute for Technology and Storage of Agricultural Products, ARO, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Falach, L., Institute of Plant Protection, Agriculture Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Zada, A., Institute of Plant Protection, Agriculture Research Organization, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Roelofs, W., Department of Entomology, Cornell University, Geneva, NY 11456, United States
Rafaeli, A., Institute for Technology and Storage of Agricultural Products, ARO, Volcani Center, P.O. Box 6, Bet Dagan, 50250, Israel
Pheromone biosynthetic pathways: PBAN-regulated rate-limiting steps and differential expression of desaturase genes in moth species
We combine the use of labeled precursors with enzyme inhibitors to decipher the biosynthetic pathway of pheromone biosynthesis and the rate-limiting step/s that are regulated by pheromone biosynthesis activating neuropeptide (PBAN). We demonstrate that Plodia interpunctella is able to utilize hexadecanoic acid, and to a lesser extent tetradecanoic acid, for the biosynthesis of the main pheromone component (Z,E)-9,12-tetradecadienyl acetate. This indicated that the main pathway involves a Δ11 desaturase, chain shortening, followed by a Δ12 desaturase, but that a functional Δ9 desaturase could also be utilized. Using reverse transcription-quantitative real-time polymerase chain reaction (RT-QPCR) we distinguish two out of nine possible desaturase gene transcripts in P. interpunctella that are expressed at the highest levels. The rate-limiting step for PBAN-stimulation was studied in two moth species so as to compare the biosynthesis of a diene (P. interpunctella) and a monoene (Helicoverpa armigera) main pheromone component. In both species, incorporation of label from the 13C sodium acetate precursor was activated by PBAN whereas no stimulatory action was observed in the incorporation of the precursors: 13C malonyl coenzyme A; hexadecanoic 16,16,16-2H3 or tetradecanoic 14,14,14-2H3 acids. The acetyl coenzyme A carboxylase (ACCase) inhibitor, Tralkoxydim, inhibited the PBAN-stimulation of incorporation of stable isotope whereas the fatty-acyl reductase inhibitor, Mevastatin, failed to influence the stimulatory action of PBAN. These results provide irrefutable support to the hypothesis that PBAN affects the production of malonyl coenzyme A from acetate by the action of ACCase in the pheromone glands of these moths. © 2008 Elsevier Ltd. All rights reserved.
Scientific Publication
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