Chapter 12 Controlled expression of iron-sulfur cluster assembly components for respiratory chain complexes in mammalian cells.
Methods Enzymol
; 456: 209-31, 2009.
Article
em En
| MEDLINE
| ID: mdl-19348891
ABSTRACT
Three of the respiratory chain complexes contain essential iron-sulfur (Fe/S) cluster prosthetic groups. Besides respiration, these ancient inorganic cofactors are also necessary for numerous other fundamental biochemical processes in virtually every known organism. Both the synthesis of Fe/S clusters and their delivery to apoproteins depend on the concerted function of specialized, often dedicated, proteins located in the mitochondria and cytosol of eukaryotes. Impaired function of the mitochondria-located Fe/S cluster (ISC) assembly machinery affects all cellular Fe/S proteins, including enzymes of the respiratory chain, NADH ubiquinone oxidoreductase (complex I; eight Fe/S clusters), succinate ubiquinone oxidoreductase (complex II; three Fe/S clusters), and cytochrome bc(1) complex (complex III; one Fe/S cluster). Here, we describe strategies and techniques both to deprive respiratory chain proteins of their Fe/S cofactors and to study changes in activity and composition of these proteins. As examples, we present the results of the depletion of two types of Fe/S biogenesis proteins, huNfs1 and huInd1, in a human tissue culture model. The ISC assembly component huNfs1 is required for biogenesis of all cellular Fe/S proteins, its loss exerting pleiotropic effects, whereas huInd1 is specific for Fe/S cluster maturation of complex I. Disorders in Fe/S cluster assembly are candidate causes for defects in respiratory complex assembly of unknown etiology.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Complexo I de Transporte de Elétrons
/
Proteínas Ferro-Enxofre
Limite:
Humans
Idioma:
En
Revista:
Methods Enzymol
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Alemanha