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 journalArticle

3 Citations (Scopus)

Abstract

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
Volume361
Issue number4
DOIs
StatePublished - Oct 5 2007

Fingerprint

Oligomerization
Proteins
Apoptosis
Caspase 1
Apoptosis Regulatory Proteins
Circular Dichroism
Oligomers
Caspase 3
Monomers
Ions
Lipids

Keywords

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

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Oligomerization of BH4-truncated Bcl-xL in solution. / Wang, Youli; Cao, Rong; Liu, Dongxiang; Chervin, Adam; Yuan, Jian; An, Jing; Huang, Ziwei.

In: Biochemical and Biophysical Research Communications, Vol. 361, No. 4, 05.10.2007, p. 1006-1011.

Research output: Contribution to journalArticle

Wang, Youli ; Cao, Rong ; Liu, Dongxiang ; Chervin, Adam ; Yuan, Jian ; An, Jing ; Huang, Ziwei. / Oligomerization of BH4-truncated Bcl-xL in solution. In: Biochemical and Biophysical Research Communications. 2007 ; Vol. 361, No. 4. pp. 1006-1011.
@article{73d8464af8fd4904923405cf446b02b5,
title = "Oligomerization of BH4-truncated Bcl-xL in solution",
abstract = "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.",
keywords = "Apoptosis, BH4 domain, Bcl-2, Bcl-x, Oligomerization, Truncated Bcl-x",
author = "Youli Wang and Rong Cao and Dongxiang Liu and Adam Chervin and Jian Yuan and Jing An and Ziwei Huang",
year = "2007",
month = "10",
day = "5",
doi = "10.1016/j.bbrc.2007.07.122",
language = "English (US)",
volume = "361",
pages = "1006--1011",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "4",

}

TY - JOUR

T1 - Oligomerization of BH4-truncated Bcl-xL in solution

AU - Wang, Youli

AU - Cao, Rong

AU - Liu, Dongxiang

AU - Chervin, Adam

AU - Yuan, Jian

AU - An, Jing

AU - Huang, Ziwei

PY - 2007/10/5

Y1 - 2007/10/5

N2 - 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.

AB - 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.

KW - Apoptosis

KW - BH4 domain

KW - Bcl-2

KW - Bcl-x

KW - Oligomerization

KW - Truncated Bcl-x

UR - http://www.scopus.com/inward/record.url?scp=34547882802&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34547882802&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2007.07.122

DO - 10.1016/j.bbrc.2007.07.122

M3 - Article

C2 - 17692289

AN - SCOPUS:34547882802

VL - 361

SP - 1006

EP - 1011

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 4

ER -