2015 Fiscal Year Final Research Report
Structure and function of bacterial lipid domains
| Project/Area Number |
24570003
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
Genetics/Genome dynamics
|
|---|
| Research Institution | Saitama University |
|---|
Principal Investigator |
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
HARA Hiroshi 埼玉大学, 理工学研究科, 准教授 (00173071)
MATSUOKA Satoshi 埼玉大学, 理工学研究科, 助教 (90509283)
|
|---|
| Research Collaborator |
SADAIE Yoshito
HASHIMOTO Michihiro
KUSAKA Jin
SHUTO Satoshi
ISHIKAWA Kazuki
IMAI Yukiko
TANIGUCHUI Aya
ITOU Aya
MIYAGAWA Hiroyoshi
UMEKAWA Mitsuru
KONDO Daitetsu
SEYA Manato
MINESHIMA Ryota
MIYAMATSU Saori
MATSUSHIMA Wakana
SEKI Takahiro
NISHINO Yuki
FURUKAWA Yugo
SAITO Tomo
NATORI Kohei
|
|---|
| Project Period (FY) |
2012-04-01 – 2016-03-31
|
| Keywords | 脂質ドメイン / カルジオリピン / ホスファチジルエタノールアミン / 枯草菌 / カルジオリピン合成酵素 / MinD / 膜結合配列 |
|---|
| Outline of Final Research Achievements |
To clarify the structure and function of bacterial lipid domains, we have adopted following two approaches. i) To elucidate the mechanism of formation of cardiolipin domain in Bacillus subtilis cells, the function of C-terminal α-helices of cardiolipin synthase is examined for septal membrane localization by fluorescence microscopy and Western blotting using GFP-ClsA fusion proteins. The enzyme is shown to be septally localized by means of its C-terminal α-helices, indicating that the C-terminal α-helices of the enzyme have a function of membrane targeting. ii) B. subtilis MinD is examined for septal localization in minJ mutant cells and is shown to be septally localized by means of the membrane targeting sequence at its C-terminus. This indicates that a correction in the current model of the sequential interaction for MinD binding to septal membranes is required.
|
| Free Research Field |
生物学分野 基礎生物学
|
