| Project/Area Number |
24770191
|
|---|
| Research Category |
Grant-in-Aid for Young Scientists (B)
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
Cell biology
|
|---|
| Research Institution | Rikkyo University (2013)
National Institute of Genetics (2012) |
|---|
Principal Investigator |
|
|---|
| Project Period (FY) |
2012-04-01 – 2014-03-31
|
| Project Status |
Completed (Fiscal Year 2013)
|
| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2013: ¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2012: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
|
|---|
| Keywords | 細胞形態 / 細胞骨格 / 大腸菌 / 抑圧変異体 / 形態形成 / 細胞骨格タンパク質 / ペプチドグリカン / タンパク質間相互作用 / Bacterial two-hybrid |
|---|
| Research Abstract |
Purpose of this project was to understand molecular mechanism to regulate bacterial cell shape. Analyses of the suppressor mutants of the rodZ mutant suggested that RodZ regulates assembly of MreB filaments. This result was published in 2012. In order to analyze the importance of the positively-charged residues in the juxta-membrane domain, I introduced Alanine into the residues and deleted the domain. I found that the positively-charged residues is dispensable for the RodZ function while the length of the domain is critical. I also analyzes the interaction among proteins constituting supramolecular machinery, elongasome. I found that RodZ interacts with MreB, MreC, PBP2, and RodA and that there are two sub-complexes in the complex, that is, MreB/MreC and PBP2/RodA complexes. The results indicate that RodZ bridges the sub-complexes. I also applied site-specific in vivo photo crosslink assay to detect interaction between RodZ and other proteins. I could detect crosslinked products.
|
