| Project/Area Number |
14380330
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Molecular biology
|
|---|
| Research Institution | Kyushu University |
|---|
Principal Investigator |
KATAYAMA Tsutomu Kyushu University, Faculty of Pharmaceutical Sciences, Prof., 大学院・薬学研究院, 教授 (70264059)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
NIKI Hironori Kyushu University, National Institute of Genetic, Assoc.Prof., 放射線アイソトープセンター, 助教授 (70208122)
|
|---|
| Project Period (FY) |
2002 – 2003
|
| Project Status |
Completed (Fiscal Year 2003)
|
| Budget Amount *help |
¥15,300,000 (Direct Cost: ¥15,300,000)
Fiscal Year 2003: ¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2002: ¥11,700,000 (Direct Cost: ¥11,700,000)
|
|---|
| Keywords | DNA replication / Cell cycle / DnaA protein / E.coli / DNA polymerase / AAA+ motif / ATP / Antibiotics / 大腸菌 |
|---|
| Research Abstract |
In the E.coli cell cycle, function of the chromosomal replication initiator DnaA protein is tightly regulated. After the ATP-bound DnaA initiates replication, DnaA-ATP is hydrolyzed by the DNA-loaded clamp subunit of DNA polymerase III holoenzyme and Hda protein, yielding ADP-bound DnaA, the inactivated form. In this study, we analyzed structure-function relationship of Hda protein, and found that the camp-binding site on Hda. Moreover, we identified important amino acid residues in AAA+ motifs of this protein. In the cell cycle, ADP-DnaA is probably reactivated for the next round of initiation of chromosomal replication. We hypothesized that an unknown factor releases ADP from DnaA. As concentration of ATP is 10-fold higher than ADP in the cell, ATP can bind to DnaA, reactivating this protein. As a result of comprehensive biochemical search, we identified a candidate of such DnaA-reactivating factor.
|
