| Project/Area Number |
26440077
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
Biophysics
|
|---|
| Research Institution | Osaka University |
|---|
Principal Investigator |
|
|---|
| 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
|
|---|
| Project Period (FY) |
2014-04-01 – 2017-03-31
|
| Project Status |
Completed (Fiscal Year 2016)
|
| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2016: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2015: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2014: ¥3,120,000 (Direct Cost: ¥2,400,000、Indirect Cost: ¥720,000)
|
|---|
| Keywords | 光制御 / 転写因子 / 光遺伝学 / LOVドメイン / bZIPドメイン / 光スイッチ / 分子間相互作用 |
|---|
| 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.
|
