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Rev Physiol Biochem Pharmacol. 2018;174:25-65. doi: 10.1007/112_2017_5.

Iron-Sulfur Protein Assembly in Human Cells.

Author information

1
Department of Biochemistry, Indian Institute of Science, C V Raman Avenue, Bengaluru, 560012, Karnataka, India.
2
Department of Biochemistry, Indian Institute of Science, C V Raman Avenue, Bengaluru, 560012, Karnataka, India. patrick@biochem.iisc.ernet.in.

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.

KEYWORDS:

Chaperones; Fe-S biogenesis; Iron-sulfur clusters; Iron-transfer; Mitochondria

PMID:
28828516
DOI:
10.1007/112_2017_5

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