A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins.
Proc Natl Acad Sci U S A
; 97(3): 1050-5, 2000 Feb 01.
Article
in En
| MEDLINE
| ID: mdl-10655482
ABSTRACT
Iron-sulfur (Fe/S) cluster-containing proteins catalyze a number of electron transfer and metabolic reactions. The components and molecular mechanisms involved in the assembly of the Fe/S clusters have been identified only partially. In eukaryotes, mitochondria have been proposed to execute a crucial task in the generation of intramitochondrial and extramitochondrial Fe/S proteins. Herein, we identify the essential ferredoxin Yah1p of Saccharomyces cerevisiae mitochondria as a central component of the Fe/S protein biosynthesis machinery. Depletion of Yah1p by regulated gene expression resulted in a 30-fold accumulation of iron within mitochondria, similar to what has been reported for other components involved in Fe/S protein biogenesis. Yah1p was shown to be required for the assembly of Fe/S proteins both inside mitochondria and in the cytosol. Apparently, at least one of the steps of Fe/S cluster biogenesis within mitochondria requires reduction by ferredoxin. Our findings lend support to the idea of a primary function of mitochondria in the biosynthesis of Fe/S proteins outside the organelle. To our knowledge, Yah1p is the first member of the ferredoxin family for which a function in Fe/S cluster formation has been established. A similar role may be predicted for the bacterial homologs that are encoded within iron-sulfur cluster assembly (isc) operons of prokaryotes.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Fungal Proteins
/
Adrenodoxin
/
Saccharomyces cerevisiae Proteins
/
Ferredoxins
/
Iron-Sulfur Proteins
/
Mitochondria
Type of study:
Prognostic_studies
Language:
En
Journal:
Proc Natl Acad Sci U S A
Year:
2000
Document type:
Article
Affiliation country:
Alemania