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Iron-Sulfur Protein Assembly in Human Cells

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Reviews of Physiology, Biochemistry and Pharmacology Vol. 174

Part of the book series: Reviews of Physiology, Biochemistry and Pharmacology ((REVIEWS,volume 174))

Abstract

Iron-sulfur (Fe-S) clusters serve as a fundamental inorganic constituent of living cells ranging from bacteria to human. The importance of Fe-S clusters is underscored by their requirement as a co-factor for the functioning of different enzymes and proteins. The biogenesis of Fe-S cluster is a highly coordinated process which requires specialized cellular machinery. Presently, understanding of Fe-S cluster biogenesis in human draws meticulous attention since defects in the biogenesis process result in development of multiple diseases with unresolved solutions. Mitochondrion is the major cellular compartment of Fe-S cluster biogenesis, although cytosolic biogenesis machinery has been reported in eukaryotes, including in human. The core biogenesis pathway comprises two steps. The process initiates with the assembly of Fe-S cluster on a platform scaffold protein in the presence of iron and sulfur donor proteins. Subsequent process is the transfer and maturation of the cluster to a bonafide target protein. Human Fe-S cluster biogenesis machinery comprises the mitochondrial iron-sulfur cluster (ISC) assembly and export system along with the cytosolic Fe-S cluster assembly (CIA) machinery. Impairment in the Fe-S cluster machinery components results in cellular dysfunction leading to various mitochondrial pathophysiological consequences. The current review highlights recent developments and understanding in the domain of Fe-S cluster assembly biology in higher eukaryotes, particularly in human cells.

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Acknowledgements

We express our sincere gratitude to the members of our group for the critical reading and review of the manuscript. We greatly acknowledge Department of Science and Technology for Swarnajayanthi fellowship (Grant ID: DST/SJF/LSA-01/2011–2012), DBT-IISc partnership programme (Grant ID: DBT/BF/PR/INS/2011-12/IISc), DST-FIST programme (Grant ID: SR/FST/LSII-544 023/2009), and UGC-CAS SAP-II programme (Grant ID: UGC LT. No. F. 5-2/2012. SAP-II) to P.D.S. We also acknowledge CSIR-India for SRF to P.P.S and K.B. We apologize to all colleagues and fellow researchers of the related domain whose original work could not be discussed or cited owing to length limitations.

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  1. Department of Biochemistry, Indian Institute of Science, C V Raman Avenue, Bengaluru, 560012, Karnataka, India

    Prasenjit Prasad Saha, Vinaya Vishwanathan, Kondalarao Bankapalli & Patrick D’Silva

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  1. Prasenjit Prasad Saha
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  2. Vinaya Vishwanathan
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  3. Kondalarao Bankapalli
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  4. Patrick D’Silva
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Correspondence to Patrick D’Silva .

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  1. Department of Cellular and Molecular Medicine, KU Leuven, Leuven, Belgium

    Bernd Nilius

  2. Heart Science Centre, The Magdi Yacoub Institute, Harefield, United Kingdom

    Pieter de Tombe

  3. Walther-Straub Institute for Pharmacology and Toxicology, Ludwig-Maximilians University of Munich, Munich, Germany

    Thomas Gudermann

  4. Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany

    Reinhard Jahn

  5. Department of Cytobiology, University of Marburg , Marburg, Germany

    Roland Lill

  6. Cardiff School of Biosciences, Cardiff University, Cardiff, United Kingdom

    Ole H. Petersen

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Saha, P.P., Vishwanathan, V., Bankapalli, K., D’Silva, P. (2017). Iron-Sulfur Protein Assembly in Human Cells. In: Nilius, B., de Tombe, P., Gudermann, T., Jahn, R., Lill, R., Petersen, O. (eds) Reviews of Physiology, Biochemistry and Pharmacology Vol. 174. Reviews of Physiology, Biochemistry and Pharmacology, vol 174. Springer, Cham. https://doi.org/10.1007/112_2017_5

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