Abstract：
:O(2) is the ultimate electron acceptor for mitochondrial respiration, a process catalyzed by cytochrome c oxidase (COX). In yeast, COX subunit composition is regulated by COX5a and COX5b gene transcription in response to high and low O(2), respectively. Here we demonstrate that in mammalian cells, expression of the COX4-1 and COX4-2 isoforms is O(2) regulated. Under conditions of reduced O(2) availability, hypoxia-inducible factor 1 (HIF-1) reciprocally regulates COX4 subunit expression by activating transcription of the genes encoding COX4-2 and LON, a mitochondrial protease that is required for COX4-1 degradation. The effects of manipulating COX4 subunit expression on COX activity, ATP production, O(2) consumption, and reactive oxygen species generation indicate that the COX4 subunit switch is a homeostatic response that optimizes the efficiency of respiration at different O(2) concentrations. Thus, mammalian cells respond to hypoxia by altering COX subunit composition, as previously observed in yeast, but by a completely different molecular mechanism.
journal_name
Celljournal_title
Cellauthors
Fukuda R,Zhang H,Kim JW,Shimoda L,Dang CV,Semenza GLdoi
10.1016/j.cell.2007.01.047subject
Has Abstractpub_date
2007-04-06 00:00:00pages
111-22issue
1eissn
0092-8674issn
1097-4172pii
S0092-8674(07)00307-8journal_volume
129pub_type
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