| Project/Area Number |
11470486
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Biological pharmacy
|
|---|
| Research Institution | OKAYAMA UNIVERSITY |
|---|
Principal Investigator |
TSUCHIYA Tomofusa (2000-2002) Faculty of Pharmaceutical Sciences Professor, 薬学部, 教授 (80012673)
黒田 照夫 (1999) 岡山大学, 遺伝子実験施設, 助手 (80304327)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
KURODA Teruo Gene research center Research Associate, 遺伝子実験施設, 助手 (80304327)
MIO Mitsunobu The graduate school of natural science and technology Associate Professor, 大学院・自然科学研究科, 助教授 (70190600)
MIZUSHIMA Tohru Faculty of Pharmaceutical Sciences Associate Professor, 薬学部, 助教授 (00264060)
KOBAYASHI Sakae Faculty of Pharmaceutical Sciences Associate Professor, 薬学部, 助教授 (90212654)
MASUDA Kazuhumi Faculty of Pharmaceutical Sciences Research Associate, 薬学部, 助手 (00243486)
月原 冨武 大阪大学, 蛋白質研究所, 教授 (00032277)
土屋 友房 岡山大学, 薬学部, 教授 (80012673)
|
|---|
| Project Period (FY) |
1999 – 2002
|
| Project Status |
Completed (Fiscal Year 2002)
|
| Budget Amount *help |
¥12,300,000 (Direct Cost: ¥12,300,000)
Fiscal Year 2002: ¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 2001: ¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 2000: ¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 1999: ¥3,300,000 (Direct Cost: ¥3,300,000)
|
|---|
| Keywords | DNA replication / DnaA / ADP / ATP / regulation of activity / ATPase / リン脂質 / ORC / 酸性リン脂質 / 機能ドメイン / 結晶構造解析 / 癌 / 開始因子 / ATP結合 / Cdc6p |
|---|
| Research Abstract |
DnaA protein, the initiator for chromosomal DNA replication in Escherichia coli, has various activities, such as oligomerization (DnaA-DnaA interaction), ATP binding. ATPase activity and membrane-binding. Site-directed mutational analyses have revealed not only the amino acid residues that are essential for these activities but also the functions of these activities. Following is a summary of the functions and regulatory mechanisms of DnaA protein in the initiation of chromosomal DNA replication. ATP-bound DnaA protein, but not other forms of the protein binds to the origin of DNA replication and forms oligomers to open-up the duplex DNA. This oligomerization is mediated by a DnaA-DnaA interaction through the N-terminal region of the protein. Alter initiation of DNA replication, the ATPase activity of DnaA protein is stimulated and DnaA protein is inactivated to the ADP-bound form to suppress the re-initiation of DNA replication. DnaA protein binds to acidic phospholipids through an ionic interaction between basic amino acid residues of the protein and acidic residues of phospholipids. This interaction seems to be involved in the re-activation of DnaA protein (from the ADP-bound form to the ATP-bound form) to initiate DNA replication after the appropriate interval.
|
