Abstract
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.
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