1987 Fiscal Year Final Research Report Summary
Molecular mechanism of biological time keeping from the viewpoint of structural change in esterase A_4 emzyme protein
Project/Area Number |
61560065
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Research Category |
Grant-in-Aid for General Scientific Research (C)
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Allocation Type | Single-year Grants |
Research Field |
蚕糸学
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Research Institution | Tottori University |
Principal Investigator |
KAI Hidenori Tottori University, Faculty of Agriculture, 農学部, 助教授 (60023412)
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Co-Investigator(Kenkyū-buntansha) |
MAEDA Susumu Tottori University Faculty of Agriculture, 農学部, 助手 (30116371)
KOBARA Ryuzo Tottori University, Faculty of Agriculture, 農学部, 教授 (70032092)
KAWAI Jakashi Tottori University, Faculty of Agriculture, 農学部, 教授 (80032043)
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Project Period (FY) |
1986 – 1987
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Keywords | Esterase A_4 / Clock / Time measuring protein / Silkworm / Diapause / Activation / Cold / グアニジンーHCl |
Research Abstract |
The elevation of esterase A_4 (Ease A_4) actioicty by cold is a switching of sequential gene exression, the stimulus that initiates diapause termination or active resumption of morphogenesis in Bombyx eggs. When the inactive Ease A_4 which is purified in column form crystals from the eggo is chilled at 5゜C in vitro, the enzyme activity is suddcnly elevated two weeks after the chilling, and is followed by a rapid fall. The sudden elevation in vitiro is equivalent to that observed in vivo, which is coincident with the chilling period indispensable to break the diapause. In the combination chilling in viwo and in vitro, the enzyme was suddenly activated two weeks after the exposure to 5゜C, irrespective of its exposure in vivo or in vitro. If the Eass A_4 which had not been activated, because of short 8- day - chilling, was treated with guanidine - HCl and then underwent re-chilling, the treated enzyme rezuired an additional two weeks for the reactivation. We argue here that the Ease A_4 measures time duration in developmental switching and that the timer function is built in the protein structure.
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Research Products
(10 results)