| Project/Area Number |
05671781
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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 |
Physical pharmacy
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| Research Institution | Osaka University |
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Principal Investigator |
YAMAGATA Yuriko Osaka University, Faculty of Pharmaceutical Sciences, Research Associate, 薬学部, 助手 (40183678)
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| Project Period (FY) |
1993 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1994: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1993: ¥1,400,000 (Direct Cost: ¥1,400,000)
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| Keywords | DNA Repair Enzyme / 3-Methyladenine-DNA Glycosylase / Three-dimensional Structure |
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| Research Abstract |
Escherichia coli has two DNA repair enzymes that liberate 3-methyladenine from DNA damaged by carcinogenic and/or mutagenic alkylating agents, namely 3-methyladenine-DNA Glycosylases I and II.They are distinguishable by their molecular sizes, enzymic properties and responses to alkylating agents. An adaptive DNA repair enzyme, 3-methyladenine-DNA glycosylase II,catalyzes the release of several alkylated bases in addition to 3-methyladenine. We have determined the three-dimensional structure of 3-methyladenine-DNA glycosylase II at a 2.3* resolution. The enzyme consists of three domains, one alpha+beta fold domain and two all alpha-helical domains. The comparison of amino acid sequence with those of Bacillus subtilis and Saccharomyces cerevisiae 3-methyladenine-DNA glycosylases and mutagenic studies allow to propose that the active site is located in a cleft between domains II and III.On the other hand, a constitutive enzyme 3-methyladenine-DNA glycosylase I releases only 3-methyladenine. The crystallization of 3-methyladenine-DNA glycosylase I is in progress.
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