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Function and biogenesis of iron–sulphur proteins

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  • Roland Lill

    (Institut für Zytobiologie, Philipps-Universität Marburg)

Abstract

Iron–sulphur (Fe–S) clusters have long been recognized as essential and versatile cofactors of proteins involved in catalysis, electron transport and sensing of ambient conditions. Despite the relative simplicity of Fe–S clusters in terms of structure and composition, their synthesis and assembly into apoproteins is a highly complex and coordinated process in living cells. Different biogenesis machineries in both bacteria and eukaryotes have been discovered that assist Fe–S-protein maturation according to uniform biosynthetic principles. The importance of Fe–S proteins for life is documented by an increasing number of diseases linked to these components and their biogenesis.

Suggested Citation

  • Roland Lill, 2009. "Function and biogenesis of iron–sulphur proteins," Nature, Nature, vol. 460(7257), pages 831-838, August.
    • Handle: RePEc:nat:nature:v:460:y:2009:i:7257:d:10.1038_nature08301
    DOI: 10.1038/nature08301
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    Cited by:

    1. Jingyu Zhan & Allison Zeher & Rick Huang & Wai Kwan Tang & Lisa M. Jenkins & Di Xia, 2024. "Conformations of Bcs1L undergoing ATP hydrolysis suggest a concerted translocation mechanism for folded iron-sulfur protein substrate," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Hye-In Nam & Zaigham Shahzad & Yanniv Dorone & Sophie Clowez & Kangmei Zhao & Nadia Bouain & Katerina S. Lay-Pruitt & Huikyong Cho & Seung Y. Rhee & Hatem Rouached, 2021. "Interdependent iron and phosphorus availability controls photosynthesis through retrograde signaling," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    3. Yangang Pan & Jingyu Zhan & Yining Jiang & Di Xia & Simon Scheuring, 2023. "A concerted ATPase cycle of the protein transporter AAA-ATPase Bcs1," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    4. Sattar Soltani & Samuel M. Webb & Thomas Kroll & Kirst King-Jones, 2024. "Drosophila Evi5 is a critical regulator of intracellular iron transport via transferrin and ferritin interactions," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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