Oligomerization of BH4-truncated Bcl-xL in solution

Youli Wang, Rong Cao, Dongxiang Liu, Adam Chervin, Jian Yuan, Jing An, Ziwei Huang

Research output: Contribution to journalArticlepeer-review

2 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1006-1011
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Oct 5 2007
Externally publishedYes


  • Apoptosis
  • BH4 domain
  • Bcl-2
  • Bcl-x
  • Oligomerization
  • Truncated Bcl-x

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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