2016 Fiscal Year Final Research Report
Photoregulation of gene expression and enzymatic activity by dimerization of LOV protein
| Project/Area Number |
26440077
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Osaka University |
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Principal Investigator |
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| Research Collaborator |
IWASA Tatsuo
HIDEKI Kandori
SAKAI Takaomi
SAKAKIBARA Shunsuke
SHICHIDA Yoshinori
TERAZIMA Masahide
NAKAMURA Ryousuke
HAMADA Norio
FUKADA Yoshitaka
MARUTA Shinsaku
MINO Hiroyuki
YAMASHITA Hayato
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Keywords | 光制御 / 転写因子 / 光遺伝学 |
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| Outline of Final Research Achievements |
Photozipper (PZ) is a protein module consisting of a bZIP and a LOV domain of AUREO1. We improved measurement systems of biomolecular complexes and investigated PZ. PZ is monomeric in the dark, and blue light induces dimerization of PZ, which subsequently increases its affinity for the target DNA sequence. PZ is, therefore, assumed to be a light-activated bZIP module. Then, we found that an intramolecular interaction between ZIP and LOV probably stabilize monomeric form in the dark state, and that intermolecular interactions of ZIP-ZIP and LOV-LOV stabilizes dimeric form in the light state. PZ fused with fluorescent proteins underwent dimerization and increased its affinity for the target DNA sequence upon illumination. Our results suggested that PZ provide a new approach for regulating the gene expression and enzymatic activities.
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| Free Research Field |
生物物理学、光生物学
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