Salt-induced changes in the subunit structure of the Bacillus stearothermophilus lipoate acetyltransferase

Yuichi Shigeoka, Tetsuro Fujisawa, Satoshi Teshiba, Hisayoshi Fukumori, Kohji Yamamoto, Yutaka Banno, Yoichi Aso

研究成果: Contribution to journalArticle査読


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.

ジャーナルBioscience, Biotechnology and Biochemistry
出版ステータス出版済み - 2013

All Science Journal Classification (ASJC) codes

  • バイオテクノロジー
  • 分析化学
  • 生化学
  • 応用微生物学とバイオテクノロジー
  • 分子生物学
  • 有機化学


「Salt-induced changes in the subunit structure of the Bacillus stearothermophilus lipoate acetyltransferase」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。