Role of the C‐terminal domain of Bax and Bcl‐xL in their localization and function in yeast cells
- 29 January 1999
- journal article
- Published by Wiley in FEBS Letters
- Vol. 443 (2), 225-228
- https://doi.org/10.1016/s0014-5793(98)01661-5
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‐xL (i.e. Bcl‐xLΔ). We find that (i) BaxΔ is as efficient as full‐length Bax in promoting cytochrome c release, but Bcl‐xLΔ has remarkably reduced rescuing ability compared to full‐length Bcl‐xL; (ii) full‐length Bcl‐xL 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‐xL, suggesting that Bcl‐xL may mask the cleavage site of Bax through a direct physical interaction of the two proteins.Keywords
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