کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1936642 | 1050697 | 2007 | 6 صفحه PDF | دانلود رایگان |
BH4 domain is critical for the anti-apoptotic functions of Bcl-2 and Bcl-xL and their binding abilities with other members of the Bcl-2 family. The cleavage of the BH4 domain in Bcl-xL and Bcl-2 by caspase 1 or 3 converts the anti-apoptotic Bcl-xL and Bcl-2 into pro-apoptotic proteins that potently induce apoptosis. Herein, we report that recombinant Bcl-xL proteins without N-terminal 61 residues, His6-NΔ61-Bcl-xL-CΔ21 and NΔ61-Bcl-xL-CΔ21, form oligomers in solution, whereas Bcl-xL-CΔ21 exists as a monomer. The oligomerization of the truncated proteins is independent of protein–lipid interaction, protein concentration or the ion strength of the solution. Circular dichroism spectrum shows a significant decrease in the content of α-helices upon deletion of N-terminal residues. NΔ61-Bcl-xL-CΔ21 also loses its heterodimerization capability with the BH3 peptide derived from Bak. This newly acquired property might be linked to its ability to induce apoptosis in cells.
Journal: Biochemical and Biophysical Research Communications - Volume 361, Issue 4, 5 October 2007, Pages 1006–1011