| Project/Area Number |
08456048
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | NAGOYA UNIVERSITY |
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Principal Investigator |
MIZUNO Takeshi NAGOYA UNIVERSITY,SCHOOL OF AGRICULTURE,PROFESSOR,, 農学部, 教授 (10174038)
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| Co-Investigator(Kenkyū-buntansha) |
YAMADA Hisami NAGOYA UNIVERSITY,SCHOOL OF AGRICULTURE,ASSISTANT PROFESSOR,, 農学部, 助手 (30089859)
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| Project Period (FY) |
1996 – 1997
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| Project Status |
Completed (Fiscal Year 1997)
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| Budget Amount *help |
¥7,500,000 (Direct Cost: ¥7,500,000)
Fiscal Year 1997: ¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 1996: ¥4,500,000 (Direct Cost: ¥4,500,000)
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| Keywords | OSMOTIC REGULATION / SIGNAL TRANSDUCTION / E.COLI / YEASTS. / GENE REGULATION. / OSMOSENSOR / TRANSCRIPTION FACTOR / 浸透圧センター / 原核生物 / 真核生物 / 分裂酵母 |
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| Research Abstract |
In general, protein phosphorylation is one of the most widely used mechanisms for regulating biological processes, including intracellular signal transduction. In eukaryotes, the cascades of protein phosphorylation and dephosphorylation events involving a number of protein tyrosine or serine/threonine kinases have been well studied. In contrast, recent intensive studies revealed that bacteria have devised a quite different phosphotransfer signaling mechanism for eliciting a variety of adaptive responses to their environment. Such a bacterial signal transduction mechanism was originally referred to as a "two-component regulatory system". The mode of molecular communication between a "sensor kinase" and its cognate phospho-accepting "response regulator" is principally based on histidine-to-aspartate (His-Asp) phosphotransfer. In Escherichia coli, for example, at least thirty different sensor-regulator pairs operate in a wide variety of adaptive responses. This particular signal transduction mechanism was once thought to be restricted to prokaryotes. However, many instances have recently been uncovered in diverse eukaryotic species. Furthermore, recent studies suggested that the molecular mechanism underlying the bacterial signal transduction is not simple as, and, in fact, is more sophisticated than thought previously. The new concept should be referred to as the "multi-step His-Asp phosphotransfer signaling mechanism". In this particular project, we extensively analyzed such signal transduction mechanisms both for prokaryotic and eukaryotic microorganisms, with special reference to their osmotic regulation.
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