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Unique dimeric structure of BNip3 transmembrane domain suggests membrane permeabilization as a cell death triggerстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Bocharov Eduard V., Pustovalova Yulia E., Pavlov Konstantin V., Volynsky Pavel E., Goncharuk Marina V., Ermolyuk Yaroslav S., Karpunin Dmitry V., Schulga Alexey A., Kirpichnikov Michail P., Efremov Roman G., Maslennikov Innokenty V., Arseniev Alexander S.
- Журнал: Journal of Biological Chemistry
- Том: 282
- Номер: 22
- Год издания: 2007
- Издательство: American Society for Biochemistry and Molecular Biology Inc.
- Местоположение издательства: United States
- Первая страница: 16256
- Последняя страница: 16266
- DOI: 10.1074/jbc.M701745200
- Аннотация: BNip3 is a prominent representative of apoptotic Bcl-2 proteins with rather unique properties initiating an atypical programmed cell death pathway resembling both necrosis and apoptosis. Many Bcl-2 family proteins modulate the permeability state of the outer mitochondrial membrane by forming homo-and hetero-oligomers. The structure and dynamics of the homodimeric transmembrane domain of BNip3 were investigated with the aid of solution NMR in lipid bicelles and molecular dynamics energy relaxation in an explicit lipid bilayer. The right-handed parallel helix-helix structure of the domain with a hydrogen bond-rich His-Ser node in the middle of the membrane, accessibility of the node for water, and continuous hydrophilic track across the membrane suggest that the domain can provide an ion-conducting pathway through the membrane. Incorporation of the BNip3 transmembrane domain into an artificial lipid bilayer resulted in pH-dependent conductivity increase. A possible biological implication of the findings in relation to triggering necrosis-like cell death by BNip3 is discussed.
- Добавил в систему: Гончарук Марина Валерьевна