Unraveling the mechanism of [4Fe-4S] cluster assembly on the N-terminal cluster binding site of NUBP1.
Protein Sci
; 32(5): e4625, 2023 05.
Article
em En
| MEDLINE
| ID: mdl-36916754
ABSTRACT
[4Fe-4S]2+ cluster assembly in human cytosol requires both a [2Fe-2S] cluster chaperone being able to donate two [2Fe-2S]2+ clusters and an electron donor providing two electrons to reductively couple the two [2Fe-2S]2+ clusters into a [4Fe-4S]2+ cluster. The mechanism through which the cytosolic [4Fe-4S]2+ cluster assembly works is still not defined. Here, we show that a hetero-tetrameric complex formed by two molecules of cluster-reduced [2Fe-2S]+ 2 -anamorsin and one molecule of dimeric cluster-oxidized [2Fe-2S]2+ 2 -GLRX32 orchestrates the assembly of a [4Fe-4S]2+ cluster on the N-terminal cluster binding site of the cytosolic protein NUBP1. We demonstrate that the hetero-tetrameric complex is able to synergically provide two [2Fe-2S]2+ clusters from GLRX3 and two electrons from anamorsin for the assembly of the [4Fe-4S]2+ cluster on the N-terminal cluster binding site of NUBP1. We also showed that only one of the two [2Fe-2S] clusters bound to anamorsin, that is, that bound to the CX8 CX2 CXC motif, provides the electrons required to form the [4Fe-4S]2+ cluster. Our study contributes to the molecular understanding of the mechanism of [4Fe-4S] protein biogenesis in the cytosol.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Domínios Proteicos
/
Proteínas Ferro-Enxofre
Limite:
Humans
Idioma:
En
Revista:
Protein Sci
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2023
Tipo de documento:
Article
País de afiliação:
Itália