Dataset Information

Iron-sulfur clusters: from metals through mitochondria biogenesis to disease.

ABSTRACT: Iron-sulfur clusters are ubiquitous inorganic co-factors that contribute to a wide range of cell pathways including the maintenance of DNA integrity, regulation of gene expression and protein translation, energy production, and antiviral response. Specifically, the iron-sulfur cluster biogenesis pathways include several proteins dedicated to the maturation of apoproteins in different cell compartments. Given the complexity of the biogenesis process itself, the iron-sulfur research area constitutes a very challenging and interesting field with still many unaddressed questions. Mutations or malfunctions affecting the iron-sulfur biogenesis machinery have been linked with an increasing amount of disorders such as Friedreich's ataxia and various cardiomyopathies. This review aims to recap the recent discoveries both in the yeast and human iron-sulfur cluster arena, covering recent discoveries from chemistry to disease.

SUBMITTER: Cardenas-Rodriguez M

PROVIDER: S-EPMC6006200 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Iron-sulfur clusters: from metals through mitochondria biogenesis to disease.

Cardenas-Rodriguez Mauricio M Chatzi Afroditi A Tokatlidis Kostas K

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 20180306 4

Iron-sulfur clusters are ubiquitous inorganic co-factors that contribute to a wide range of cell pathways including the maintenance of DNA integrity, regulation of gene expression and protein translation, energy production, and antiviral response. Specifically, the iron-sulfur cluster biogenesis pathways include several proteins dedicated to the maturation of apoproteins in different cell compartments. Given the complexity of the biogenesis process itself, the iron-sulfur research area constitut ...[more]

PMID: 29511832

Similar Datasets

Project description:Iron-sulfur clusters are required in a variety of biological processes. Biogenesis of iron-sulfur clusters includes assembly of iron-sulfur clusters on scaffold complexes and transfer of iron-sulfur clusters to recipient apoproteins by iron-sulfur carriers, such as nitrogen-fixation-subunit-U (NFU)-type proteins. Arabidopsis thaliana has three plastid-targeted NFUs: NFU1, NFU2, and NFU3. We previously discovered that nfu2 -/- nfu3 -/- mutants are embryo lethal. The lack of viable nfu2 -/- nfu3 -/- mutants posed a serious challenge. To overcome this problem, we characterized nfu2-1 -/- nfu3-2+/- and nfu2-1+/- nfu3-2 -/- sesquimutants. Simultaneous loss-of-function mutations in NFU2 and NFU3 have an additive effect on the declines of 4Fe-4S-containing PSI core subunits. Consequently, the sesquimutants had much lower PSI and PSII activities, much less chlorophyll, and much smaller plant sizes, than nfu2-1 and nfu3-2 single mutants. These observations are consistent with proposed roles of NFU3 and NFU2 in the biogenesis of chloroplastic 4Fe-4S. By performing spectroscopic and in vitro reconstitution experiments, we found that NFU1 may act as a carrier for chloroplastic 4Fe-4S and 3Fe-4S clusters. In line with this hypothesis, loss-of-function mutations in NFU1 resulted in significant declines in 4Fe-4S- and 3Fe-4S-containing chloroplastic proteins. The declines of PSI activity and 4Fe-4S-containing PSI core subunits in nfu1 mutants indicate that PSI is the main target of NFU1 action. The reductions in 4Fe-4S-containing PSI core proteins and PSI activity in nfu3-2, nfu2-1, and nfu1 single mutants suggest that all three plastid-targeted NFU proteins contribute to the biogenesis of chloroplastic 4Fe-4S clusters. Although different insertion sites of T-DNA lines may cause variations in phenotypic results, mutation severity could be an indicator of the relative importance of the gene product. Our results are consistent with the hypothesis that NFU3 contributes more than NFU2 and NFU2 contributes more than NFU1 to the production of 4Fe-4S-containing PSI core subunits.

Dataset Information

Iron-sulfur clusters: from metals through mitochondria biogenesis to disease.

Publications

Iron-sulfur clusters: from metals through mitochondria biogenesis to disease.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure