| Project/Area Number |
60480501
|
|---|
| Research Category |
Grant-in-Aid for General Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
代謝生物化学
|
|---|
| Research Institution | OSAKA UNIVERSITY |
|---|
Principal Investigator |
FUTAI Masamitsu The Institute of Scientific and Industrial Research, Osaka University, 産業科学研究所, 教授 (50012646)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
MAEDA Masatomo The Institute of Scientific and Industrial Research, Osaka University, 産業科学研究所, 助手 (80190297)
AMEMURA Akinori The Institute of Scientific and Industrial Research, Osaka University, 産業科学研究所, 講師 (90029877)
SHIMOMURA Shoji The Institute of Scientific and Industrial Research, Osaka University, 産業科学研究所, 助手 (90116046)
|
|---|
| Project Period (FY) |
1985 – 1986
|
| Project Status |
Completed (Fiscal Year 1986)
|
| Budget Amount *help |
¥1,200,000 (Direct Cost: ¥1,200,000)
Fiscal Year 1986: ¥1,200,000 (Direct Cost: ¥1,200,000)
|
|---|
| Keywords | <F_o> <F_1> / ATPase / ATP Synthase / Escherichia coli / 【F_0】【F_1】 |
|---|
| Research Abstract |
The ATP synthase of Escherichia coli has essentially the same structure and functions as those found in mitochondria. The catalytic portion of the enzyme, <F_1> , consists of 5 subunits <alpha> , <beta> , <gamma> , <delta> and <epsilon> , and has ATPase activity. The <F_o> portion has three subunits, a, b and c, and functions as a proton channel. The eight subunits are encoded by the unc operon which DNA sequence was determined by our group. We isolated more than 150 mutants of unc operon and established rapid method to determine their altered amino acid residues. In this research project we studied mechanism and assembly of the enzyme at the level of amino acid residues.
(1) We have analyzed catalytic cooperativity of the enzyme using inhibitors and mutants. Our results showed that the two mechanisms uni- and multi- site catalyses of the enzyme can be clearly separated. Mutation studies indicated that Arg-246 or the region in its vicinity is important for the catalytic cooperativity.
(2) Assembly mutations (in <beta> and <gamma> subunits) were analyzed extensively, and a new model for the enzyme was proposed.
(3) Extensive analysis of mutations in <F_o> subunits was carried out. Residues participating proton relay system were proposed.
|
