Premium
Role of the C‐terminal domain of Bax and Bcl‐x L in their localization and function in yeast cells
Author(s) -
Priault Muriel,
Camougrand Nadine,
Chaudhuri Bhabatosh,
Ma Stéphen
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01661-5
Subject(s) - yeast , terminal (telecommunication) , domain (mathematical analysis) , function (biology) , microbiology and biotechnology , chemistry , c terminus , saccharomyces cerevisiae , biology , biochemistry , computer science , amino acid , computer network , mathematics , mathematical analysis
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 L Δ). We find that (i) BaxΔ is as efficient as full‐length Bax in promoting cytochrome c release, but Bcl‐x L Δ 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.