Iron–sulfur (Fe–S) clusters are ubiquitous cofactors present in all domains of life. The chemistries catalyzed by these inorganic cofactors are diverse and their associated enzymes are involved in many cellular processes. Despite the wide range of structures reported for Fe–S clusters inserted into proteins, the biological synthesis of all Fe–S clusters starts with the assembly of simple units of 2Fe–2S and 4Fe–4S clusters. Several systems have been associated with the formation of Fe–S clusters in bacteria with varying phylogenetic origins and number of biosynthetic and regulatory components. All systems, however, construct Fe–S clusters through a similar biosynthetic scheme involving three main steps: (1) sulfur activation by a cysteine desulfurase, (2) cluster assembly by a scaffold protein, and (3) guided delivery of Fe–S units to either final acceptors or biosynthetic enzymes involved in the formation of complex metalloclusters. Another unifying feature on the biological formation of Fe–S clusters in bacteria is that these systems are tightly regulated by a network of protein interactions. Thus, the formation of transient protein complexes among biosynthetic components allows for the direct transfer of reactive sulfur and Fe–S intermediates preventing oxygen damage and reactions with non-physiological targets. Recent studies revealed the importance of reciprocal signature sequence motifs that enable specific protein–protein interactions and consequently guide the transactions between physiological donors and acceptors. Such findings provide insights into strategies used by bacteria to regulate the flow of reactive intermediates and provide protein barcodes to uncover yet-unidentified cellular components involved in Fe–S metabolism.
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December 2018
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Dysfunctional cytoskeleton and neurodegeneration: novel pathways in Parkinson's disease? This image represents the degeneration of the neuronal tree during the aging process. In this issue Civiero et al. discuss the consequence of impaired cytoskeletal dynamics on neurite morphology and neuronal physiology in Parkinson's disease. For further details see pages 1653–1663.
Review Article|
October 31 2018
Metallocluster transactions: dynamic protein interactions guide the biosynthesis of Fe–S clusters in bacteria
Chenkang Zheng;
Chenkang Zheng
1Center for Molecular Signaling, Department of Chemistry, Wake Forest University, Winston-Salem, NC 27101, U.S.A.
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Patricia C. Dos Santos
1Center for Molecular Signaling, Department of Chemistry, Wake Forest University, Winston-Salem, NC 27101, U.S.A.
Correspondence: Patricia C. Dos Santos (dossanpc@wfu.edu)
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Publisher: Portland Press Ltd
Received:
August 08 2018
Revision Received:
September 12 2018
Accepted:
September 14 2018
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2018 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2018
Biochem Soc Trans (2018) 46 (6): 1593–1603.
Article history
Received:
August 08 2018
Revision Received:
September 12 2018
Accepted:
September 14 2018
Citation
Chenkang Zheng, Patricia C. Dos Santos; Metallocluster transactions: dynamic protein interactions guide the biosynthesis of Fe–S clusters in bacteria. Biochem Soc Trans 17 December 2018; 46 (6): 1593–1603. doi: https://doi.org/10.1042/BST20180365
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