Salt-Induced Changes in the Subunit Structure of the Bacillus stearothermophilus Lipoate Acetyltransferase
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概要
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The Bacillus stearothermophilus lipoate acetyltransferase (E2), composed of sixty identical, subunits is the core component of the pyruvate dehydrogenase complex (PDC). E2 polypeptide is composed of LD, PSBD, and CD domains. Most studies had focused on a truncated E2 that is deficient in LD and PSBD, because CD mainly contributes to maintaining the multimeric structure. We examined salt-induced changes in E2 without truncation and constructed reaction models. We speculate that in the presence of KCl, E2 is dissociated into a monomer and then assembled into an aggregative complex (CA) and a quasi-stable complex (CQ). CA was larger than CQ, but smaller than intact E2. CA and CQ were dominant complexes at about neutral pH and at basic pH respectively. PDC, in which PSBD is occupied by other components, and a truncated E2 undergo dissociation only. LD-PSBD region besides CD might then contribute to the partial association of dissociated E2.
著者
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Yamamoto Kohji
Institute Of Genetic Resources Graduate School Of Bioresources And Bioenvironmental Science Kyushu U
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Banno Yutaka
Institute Of Genetic Resources Faculty Of Agriculture Kyushu University Graduated School
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FUJISAWA Tetsuro
Department of Biomolecular Science, Graduate School of Engineering, Gifu University
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Fujisawa Tetsuro
Department Of Biomolecular Science Graduate School Of Engineering Gifu University
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Teshiba Satoshi
Institute Of Genetic Resources Faculty Of Agriculture Kyushu University
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Shigeoka Yuichi
Institute Of Genetic Resources Faculty Of Agriculture Kyushu University
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Aso Yoichi
Institute of Genetic Resources, Faculty of Agriculture, Kyushu University
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Banno Yutaka
Institute of Genetic Resources, Faculty of Agriculture, Kyushu University
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FUKUMORI Hisayoshi
Institute of Genetic Resources, Faculty of Agriculture, Kyushu University
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