A cytochrome c-GFP fusion is not released from mitochondria into the cytoplasm upon expression of Bax in yeast cells.

Abstract:

:To study Bax-induced release of cytochrome c in vivo, we have expressed a cytochrome c-GFP (green fluorescent protein) fusion in Saccharomyces cerevisiae cells null for the expression of the endogenous cytochrome. We show here that cytochrome c-GFP is efficiently localised to mitochondria and able to function as an electron carrier between complexes III and IV of the respiratory chain. Strikingly, while natural cytochrome c is released into the cytoplasm upon expression of Bax, the cytochrome c-GFP fusion is not. Nevertheless, cells co-expressing Bax and the cytochrome c-GFP fusion die, indicating that mitochondrial release of cytochrome c is not essential for cell death to occur in yeast. The failure to release cytochrome c-GFP is presumed to arise from increased bulk due to the GFP moiety. We propose that in intact yeast cells, Bax-induced release of cytochrome c into the cytoplasm occurs through a selective pore and not as a consequence of the non-specific breakage of the mitochondrial outer membrane.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Roucou X,Prescott M,Devenish RJ,Nagley P

doi

10.1016/s0014-5793(00)01404-6

keywords:

subject

Has Abstract

pub_date

2000-04-14 00:00:00

pages

235-9

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(00)01404-6

journal_volume

471

pub_type

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