Role of the C-terminal domain of Bax and Bcl-XL in their localization and function in yeast cells.

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. BaxA) and Bcl-X(L) (i.e. Bcl-X(L)delta). We find that (i) Bax(delta) is as efficient as full-length Bax in promoting cytochrome c release, but Bcl-x(L)delta 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Priault M,Camougrand N,Chaudhuri B,Manon S

doi

10.1016/s0014-5793(98)01661-5

subject

Has Abstract

pub_date

1999-01-25 00:00:00

pages

225-8

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)01661-5

journal_volume

443

pub_type

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