期刊
Scientific Reports
卷 6, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/srep30763
关键词
-
资金
- NIH [5 R01 GM097508, R01 CA125562, RR022422, OD011937, EB001980]
- EPR Center at RFUMS
- RFUMS Start-up fund
In mitochondrial apoptosis, Bak is activated by death signals to form pores of unknown structure on the mitochondrial outer membrane via homooligomerization. Cytochrome c and other apoptotic factors are released from the intermembrane space through these pores, initiating downstream apoptosis events. Using chemical crosslinking and double electron electron resonance (DEER)-derived distance measurements between specific structural elements in Bak, here we clarify how the Bak pore is assembled. We propose that previously described BH3-in-groove homodimers (BGH) are juxtaposed via the 'alpha 3/alpha 5' interface, in which the C-termini of helices alpha 3 and alpha 5 are in close proximity between two neighboring Bak homodimers. This interface is observed concomitantly with the well-known 'alpha 6:alpha 6' interface. We also mapped the contacts between Bak homodimers and the lipid bilayer based on EPR spectroscopy topology studies. Our results suggest a model for the lipidic Bak pore, whereby the mitochondrial targeting C-terminal helix does not change topology to accommodate the lining of the pore lumen by BGH.
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