Role of the C‐terminal domain of Bax and Bcl‐xL in their localization and function in yeast cells

FEBS Letters

Priault, Muriel¹  Manon, Stéphen¹  Chaudhuri, Bhabatosh²  Camougrand, Nadine¹ 

[1] Institut de Biochimie et de Génétique Cellulaires du C.N.R.S., 1 rue Camille Saint-Saëns, F-33077 Bordeaux Cedex, France;Oncology Research, Novartis-Pharma, CH-4032 Basel, Switzerland

关键词: Apoptosis;    Bax;    Bcl-xL;    Cytochrome c;    Yeast mitochondrion;   

DOI  :  10.1016/S0014-5793(98)01661-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

It has been suggested that the C-terminal domain of Bcl-2 family members may contain a signal anchor sequence that targets these proteins to the mitochondrial outer membrane. We have investigated the consequence of deleting this domain upon cytochrome c release in yeast strains that coexpress truncated forms of Bax (i.e. BaxΔ) and Bcl-x_L (i.e. Bcl-x_LΔ). We find that (i) BaxΔ is as efficient as full-length Bax in promoting cytochrome c release, but Bcl-x_LΔ has remarkably reduced rescuing ability compared to full-length Bcl-x_L; (ii) full-length Bcl-x_L protein acts by relocalizing Bax from the mitochondrial fraction to the soluble cytosolic fraction; (iii) Bax undergoes N-terminal cleavage when expressed in yeast, which is prevented by coexpression of Bcl-x_L, suggesting that Bcl-x_L may mask the cleavage site of Bax through a direct physical interaction of the two proteins.

【 授权许可】

Unknown