| Project/Area Number |
60580212
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
分子遺伝学・分子生理学
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| Research Institution | Osaka University |
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Principal Investigator |
OGAWA Tomoko Faculty of Science, 理学部, 講師 (80028208)
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| Project Period (FY) |
1985 – 1986
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| Project Status |
Completed (Fiscal Year 1986)
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| Budget Amount *help |
¥1,900,000 (Direct Cost: ¥1,900,000)
Fiscal Year 1986: ¥300,000 (Direct Cost: ¥300,000)
Fiscal Year 1985: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | The activated form of RecA protein for the repressor cleavage / RecA protein / <phi> 80 repressor / The cleavage reaction of repressor by RecA protein / a role of the C-terminal region of RecA protein |
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| Research Abstract |
Purified RecA protein can cleave LexA protein and several prophage repressors ( <lambda> , P22 and 434 ) in vitro at a specific Ala-Gly peptide bonds in the middle of these polypeptide chains. This reaction requires single-stranded DNA, ATP (or ATP- <gamma> -S or dATP) and <Mg^(++)> . To learn what the activated form of RecA protein is and how the cleavage specificity is determined, we investigated the detail mechanisms on the cleavage reaction using <phi> 80, <lambda> and LexA repressors and RecA mutant proteins. Results showed that the RecA-mediated cleavage reaction of the repressors was controled with two processes. One is the formation of an active binary complex between RecA protein and single-stranded DNA. Another is the interaction of the active binary complex with repressor protein. The former process is likely to be controled by the C-terminal region of RecA protein, and the latter process seems to be stimulated by the conformational change of the repressor by interaction with a specific cofactor, such as dGpG or dApG.
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