N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization

N-terminal tyrosine of ISCU2 triggers [2Fe-2S] cluster synthesis by ISCU2 dimerization

[2Fe-2S] protein cofactors are essential for life and are synthesized on ISCU2 scaffolds. Here, the authors show that hydrophobic interaction of two conserved N-terminal tyrosines induces ISCU2 dimerization and concomitant [2Fe-2S] cluster synthesis.

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Detalles Bibliográficos
Autores principales: Sven-A. Freibert, Michal T. Boniecki, Claudia Stümpfig, Vinzent Schulz, Nils Krapoth, Dennis R. Winge, Ulrich Mühlenhoff, Oliver Stehling, Miroslaw Cygler, Roland Lill
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
Materias:
Science
Q
Acceso en línea:https://doaj.org/article/c031fda3199f4ae4ade00e57b4490d02
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Descripción
Sumario:[2Fe-2S] protein cofactors are essential for life and are synthesized on ISCU2 scaffolds. Here, the authors show that hydrophobic interaction of two conserved N-terminal tyrosines induces ISCU2 dimerization and concomitant [2Fe-2S] cluster synthesis.

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