2005 Fiscal Year Final Research Report Summary
Cell cycle regulation by protein degradation and transport
| Project/Area Number |
13043006
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research on Priority Areas
|
| Allocation Type | Single-year Grants |
|---|
| Review Section |
Biological Sciences
|
|---|
| Research Institution | The University of Tokyo |
|---|
Principal Investigator |
TOH-E Akio The University of Tokyo, Department of Biological Sciences, Professor, 大学院理学研究科, 教授 (90029249)
|
|---|
| Project Period (FY) |
2001 – 2005
|
| Keywords | 26S proteasome / 19S reguratory comoplex / base / baker's yeast / lid / RPN7 / RPN6 / RPN5 |
|---|
| Research Abstract |
It is widely accepted that the ubiquitin-proteasome system plays a pivotal role in degradation of short-lived proteins, many of them are regulatory proteins, in an energy dependent manner. The 26S proteasome is responsible to the final step of proteolysis in this system. The 26S proteasome is a large protein complex consisting of 20S proteasome containing active sites and 19S regulatory factor called as 19S RP. The basic subunit composition has been elucidated. By exploiting this information, we started uncovering how and where these subunits assemble together. We focused on the 19S RP of Saccharomyces cerevisiae. The 19S RP consists of two sub-complexes, the lid and the base. We isolated temperature-sensitive mutants of the genes encoding subunits of the lid. Biochemical characterization revealed that hierarchy of the assembly of the lid, and the lid and the base are constructed independently of each other. We also examined localization of each sub-complex in various mutants and found that the base and the lid can separately be localized in the nucleus. The 19S RP too is localized in the nucleus and assembles with the 20S proteasome to the 26S proteasome.
|
Research Products
(32 results)
