Mechanisms of Mitochondrial Iron-Sulfur Protein Biogenesis.
Annu Rev Biochem
; 89: 471-499, 2020 06 20.
Article
em En
| MEDLINE
| ID: mdl-31935115
ABSTRACT
Mitochondria are essential in most eukaryotes and are involved in numerous biological functions including ATP production, cofactor biosyntheses, apoptosis, lipid synthesis, and steroid metabolism. Work over the past two decades has uncovered the biogenesis of cellular iron-sulfur (Fe/S) proteins as the essential and minimal function of mitochondria. This process is catalyzed by the bacteria-derived iron-sulfur cluster assembly (ISC) machinery and has been dissected into three major steps:
de novo synthesis of a [2Fe-2S] cluster on a scaffold protein; Hsp70 chaperone-mediated trafficking of the cluster and insertion into [2Fe-2S] target apoproteins; and catalytic conversion of the [2Fe-2S] into a [4Fe-4S] cluster and subsequent insertion into recipient apoproteins. ISC components of the first two steps are also required for biogenesis of numerous essential cytosolic and nuclear Fe/S proteins, explaining the essentiality of mitochondria. This review summarizes the molecular mechanisms underlying the ISC protein-mediated maturation of mitochondrial Fe/S proteins and the importance for human disease.Palavras-chave
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Base de dados:
MEDLINE
Assunto principal:
Ataxia de Friedreich
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Chaperonas Moleculares
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Doenças Mitocondriais
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Proteínas Mitocondriais
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Proteínas Ferro-Enxofre
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Mitocôndrias
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article