2010 Fiscal Year Final Research Report
Redox- and CO-dependent Transcription Mechanism by NPAS2
| Project/Area Number |
20570121
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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 |
Functional biochemistry
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| Research Institution | Hokkaido University |
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Principal Investigator |
UCHIDA Takeshi Hokkaido University, 大学院・理学研究院, 助教 (30343742)
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| Project Period (FY) |
2008 – 2010
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| Keywords | 時計蛋白質 / 転写制御 / DNA結合 / ラマン分光法 / NPAS2 |
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| Research Abstract |
The purpose of this project is to clarify the mechanism of the redoxand CO-dependent transcription by NPAS2. By using resonance Raman technique, we found that CO can bind to heme located inside NPAS2, which leads to a small conformational change around heme peripheral groups. Such a conformational change around heme is a trigger for the protein whole structural change to modulate the affinity of NPAS2 to the target DNA.
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[Journal Article] Unusual Heme Binding in the Bacterial Iron Response Regulator Protein (Irr) : SpectralCharacterization of Heme Binding to HemeRegulatory Motif.2011
Author(s)
Ishikawa, H., Nakagaki, M., Bamba, A., Uchida T., Hori, H., O'Brian, M.R., Iwai, K., Ishimori, K.
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Journal Title
Biochemistry 50
Pages: 1016-1022
Peer Reviewed
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[Journal Article] Molecular oxygen regulates theenzymatic activity of a heme-containing diguanylate cyclase (HemDGC) for the synthesis of cyclic di-GMP2010
Author(s)
Sawai, H., Yoshioka, S., Uchida T., Hyodo, M., Hayakawa, Y., Ishimori, K., Aono, S.
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Journal Title
Biochimica et Biophysica Acta 1804
Pages: 166-172
Peer Reviewed
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