| Project/Area Number |
05670271
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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 |
Bacteriology (including Mycology)
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| Research Institution | Tokushima Bunri University |
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Principal Investigator |
SAKURAI Jun Tokushima Bunri University, Faculty of Pharmaceutical Science, Full Professor, 薬学部, 教授 (80029800)
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| Co-Investigator(Kenkyū-buntansha) |
KOBAYASHI Keiko Tokushima Bunri University, Faculty of Pharmaceutical Sciences, Research Associa, 薬学部, 助手 (90170315)
NAGAHAMA Masahiro Tokushima Bunri University, Faculty of Pharmaceutical Sciences, Assistant Profes, 薬学部, 助教授 (40164462)
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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 |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1994: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1993: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | Clostridium perfringens / alpha Toxin / Phospholipase C / Phospholipase D / Phospholipid metabolism / Site-directed-mutagenesis / Histidine / Hemolysis / ウェルシュ菌 / ガス壊疽 / alpha毒素 / GTP-結合タンパク質 / ホスファチジル4,5-二リン酸 / ホスファチジン酸 / プロテインキナーゼC |
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| Research Abstract |
We replaced all nine histidine residues in Clostridium perfringens alpha toxin with neutral amino acids (alanine, leucine and glycine) by site-direct mutagenesis and investigated the relationship between the biological activities and histidine residues or zinc ion in the toxin.The results suggested that the histidine-11 residue in the toxin is regarded as an essential and integral part of the toxin protein, that the histidine-68, -126 and 136 residues bind an exchangeable and labile divalent metal which is important for binding to membranes and substrates and that the histidine-148 residue tightly binds one zinc metal which is essential for the active or catalytic site of alpha toxin.
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