Molecular Anatomy of Transcription Apparatus
Project/Area Number |
07044106
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Research Category |
Grant-in-Aid for international Scientific Research
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Allocation Type | Single-year Grants |
Section | Joint Research |
Research Institution | National Institute of Genetics |
Principal Investigator |
ISHIHAMA Akira National Institute of Genetics, Department of Molecular Genetics Professor, 分子遺伝研究系, 教授 (80019869)
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Co-Investigator(Kenkyū-buntansha) |
BUSBY Steve University of Birmingham, School of Biochemistry, 生化学部, 教授
HAYWARP Rich エジンバラ大学, 細胞分子生物学研究所, 教授
CLASS Robert E. University of Nottingham, School of Medicine, 医学部, 教授
FUJITA Nobuyuki National Institute of Genetics, Department of Molecular Genetics, 分子遺伝研究系, 助手 (90173434)
HAYWARD Richard S. University of Edinburgh, Institute of Cell and Molecular Biology
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Project Period (FY) |
1995
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Project Status |
Completed (Fiscal Year 1995)
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Budget Amount *help |
¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 1995: ¥1,900,000 (Direct Cost: ¥1,900,000)
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Keywords | RNA polymerase / Transcription apparatus / Transcription regulation / Transcription factor / Molecular anatomy / Protein structure / Genetic analysis / Molecular assembly |
Research Abstract |
The promoter selectivity of Escherichia coli RNA polymerase is determined by two steps of molecular interaction with transcription factors : (1) association of core enzyme with one of various sigma subunits, each recognizing a group of unique promoters, to constitute different forms of holoenzyme ; and (2) association of holoenzyme with one of about 100 species of accessory transcription factors.The intracellular concentration of each sigma subunit was determined using a quantitative immunoblot method.Results indicate that the concentration of sigma subunits and their affinity to core enzyme are subject to control depending on the cell growth conditions.In order to reveal the second step modulation of RNA polymerase specificity, the contact site on RNA polymerase was determined for more than 20 transcription factors.Results indicate that each factor interacts with RNA polymerase at a narrow region consisting of about 10 amino acid residues and that the contact sites are clustered within a regulatory domain of each subunit.Fine mapping has been done for the contact sites on alpha subunit with class-I factors.Furthermore, the contact surface of the class-I factor on the alpha subunit was found to participate in binding DNA enhancer element.
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Report
(1 results)
Research Products
(10 results)