| Project/Area Number |
05640729
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
植物生理
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
MESHI Tetsuo Kyoto University, Faculty of Science, Associate Professor, 理学部, 助教授 (40157813)
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| Co-Investigator(Kenkyū-buntansha) |
NAKAYAMA Takuya Kyoto Univ., Fac.Sci.Res.Associate, 理学部, 助手 (30207948)
IWABUCHI Masaki Kyoto Univ., Fac.Sci.Professor, 理学部, 教授 (30000839)
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| Project Period (FY) |
1993 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
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| Budget Amount *help |
¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1994: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1993: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | histone gene / interaction / transcription regulation / bZIP-type factor / transcription factor / HBP-1a |
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| Research Abstract |
To identify the components involved in the formation of the special complex on the type I element in the wheat histone H3 promoter, which is known to confer the S-phase specific transcription, we carried out West-western screening with phosphorylated HBP-1a (17) as a probe. Aa a result, a novel bZIP-type transcription factor, HALF-1, was isolated from wheat cDNA library. With GST-fusions and by gel shift analysis, HALF-1 and HBP-1a (17) were demonstrated to interact with each other through their ZIP domains. Northern analysis revealed that HALF-1 expressed highly in the late S to early G2 phases. Transient assay revealed that HALF-1 had a potential activation domain that contained an amino acid stretch conserved among several plant bZIP proteins. The DNA-binding specificity and the structural characteristics showed that HALF-1 belonged to the HBP-1a subfamily.
Wheat nuclear extracts prepared from S phase cells contained some specific DNA-binding activity directing to the hexamer motif and to the octamer motif. The S-phase specific hexamer-binding activity had the character similar to that of the HBP-1a subfamily and was suggested to be regulated by phosphorylation.
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