Research on Mechanism of Activating a Promoter by Bent DNA and it's Application
| Project/Area Number |
13670274
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Bacteriology (including Mycology)
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| Research Institution | Okayama University of Science |
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Principal Investigator |
KATAYAMA Seiichi Okayama University of Science Faculty of Science, Biochemisry, Assistant Professor, 理学部, 講師 (70169473)
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| Project Period (FY) |
2001 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2002: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2001: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | Clostridium perfringens / phospholipase C / transcriptional regulation / phased A-tracts / bent DNA / RNA polymerase / α subunit / reconstitution / Clostridum perfringens |
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| Research Abstract |
Previously we showed that the expression of a Clostridium perfringens phospholipase C gene (plc) is activated by promoter upstream phased A-tracts in a low temperature-dependent manner. In this research we characterize the interaction between the α subunit of C. perfringens RNA polymerase and the phased A-tracts. Hydroxyl radical footprinting and fluorescence polarization assaying revealed that the α subunit binds to the minor grooves of the phased A- tracts through its C-terminal domain with increased affinity at low temperature. The result provides a molecular mechanism underlying the activation of the plc promoter by phased A-tracts
In order to clarify the contribution of the C-terminal domain of the α subunit on plc promoter activation, we tried to reconstitute of C. perfringens RNA polymerase, lacking the C-terminal domain. But we could not get any active RNA polymerase reconstituted with recombinant α, β, β', and o subunits of C. perfringens
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Report
(3 results)
Research Products
(3 results)
