Biogenesis of Iron-Sulfur Clusters in Photosystem I

Zhao, Jun; Heinnickel, Mark; Krebs, Carsten; Shen, Gaozhong; Golbeck, John H.; Bryant, Donald A.

doi:10.1074/jbc.m803395200

Cited by 37 publications

(19 citation statements)

References 44 publications

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“…Monothiol glutaredoxins and Nfu-like proteins have also been implicated in trafficking Fe-S clusters from scaffolds to target proteins. (Angelini et al , 2008, Bandyopadhyay et al , 2008, Jin et al , 2008, Py et al , 2012, Zimbler et al , 2012, Haussig et al , 2013, Mapolelo et al , 2013) In some systems the suf operon has its own dedicated transcriptional regulator while in other cases the suf pathway is controlled by multiple regulators that respond to stresses that disrupt Fe-S cluster metabolism. (Patzer & Hantke, 1999, Zheng et al , 2001, Lee et al , 2004, Outten et al , 2004, Wang et al , 2004, Yeo et al , 2006, Shen et al , 2007, Nesbit et al , 2009)…”

Section: The Suf Fe-s Cluster Biogenesis System: An Overviewmentioning

confidence: 99%

Recent advances in the Suf Fe–S cluster biogenesis pathway: Beyond the Proteobacteria

Outten

2015

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Fe-S clusters play critical roles in cellular function throughout all three kingdoms of life. Consequently, Fe-S cluster biogenesis systems are present in most organisms. The Suf (sulfur formation) system is the most ancient of the three characterized Fe-S cluster biogenesis pathways, which also include the Isc and Nif systems. Much of the first work on the Suf system took place in Gram-negative Proteobacteria used as model organisms. These early studies led to a wealth of biochemical, genetic, and physiological information on Suf function. From those studies we have learned that SufB functions as an Fe-S scaffold in conjunction with SufC (and in some cases SufD). SufS and SufE together mobilize sulfur for cluster assembly and SufA traffics the complete Fe-S cluster from SufB to target apo-proteins. However, recent progress on the Suf system in other organisms has opened up new avenues of research and new hypotheses about Suf function. This review focuses primarily on the most recent discoveries about the Suf pathway and where those new models may lead the field.

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Section: The Suf Fe-s Cluster Biogenesis System: An Overviewmentioning

confidence: 99%

Recent advances in the Suf Fe–S cluster biogenesis pathway: Beyond the Proteobacteria

Outten

2015

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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“…Examples include the following: CyaY, an iron-binding protein believed to be involved in iron trafficking and iron delivery (5-7); YggX, an Fe 2ϩ -binding protein that protects the cell from oxidative stress (8,9); ErpA, an alternate A-type [Fe-S] cluster scaffolding protein (10); NfuA, a proposed intermediate [Fe-S] delivery protein (11)(12)(13); YtfE, a protein proposed to be involved in [Fe-S] cluster repair (14,15); and CsdA-CsdE, an alternative cysteine desulferase (16).…”

Section: Nifusvcyse1) Involved In the Biosynthesis Of [Fe-s] Clustersmentioning

confidence: 99%

Bacterial ApbC Protein Has Two Biochemical Activities That Are Required for in Vivo Function

Boyd

Sondelski

Downs

2009

Journal of Biological Chemistry

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Analysis of the metabolic network anchored to thiamine biosynthesis in S. enterica identified lesions in three non-isc or -suf loci that compromise Fe-S metabolism as follows: apbC, apbE, and rseC (17-21). This metabolic system was subsequently used to dissect a role for cyaY and gshA in [Fe-S] cluster metabolism (6,22,23). Of these, the apbC (mrp in E. coli) locus was identified as the predominant site of lesions that altered thiamine synthesis by disrupting [Fe-S] cluster metabolism (17,18).ApbC is a member of the ParA subfamily of proteins that have a wide array of functions, including electron transfer (24), initiation of cell division (25), and DNA segregation (26,27). Importantly, ATP hydrolysis is required for function of all well characterized members of this subfamily, and all members contain a "deviant" Walker A motif, which contains two lysine residues instead of one (GKXXXGK(S/T)) (28). ApbC has been shown to hydrolyze ATP (17).Recently, five proteins with a high degree of identity to ApbC have been shown to be involved in [Fe-S] cluster metabolism in eukaryotes. The sequence alignments of the central portion of these proteins and bacterial ApbC are shown in Fig. 1. HCF101 was demonstrated to be involved in chloroplast [Fe-S] cluster metabolism (29, 30). The CFD1, Npb35, and huNbp35 (formally Nubp1) proteins were demonstrated to be involved in cytoplasmic [Fe-S] cluster metabolism (31,32). Ind1 was demonstrated to be involved in the maturation of [Fe-S] clusters in the mitochondrial enzyme NADH:ubiquinone oxidoreductase (33). There is currently no report of any of these proteins hydrolyzing ATP.Biochemical analysis of ApbC indicated that it could bind and transfer [Fe-S] clusters to Saccharomyces cerevisiae apo-isopropylmalate isomerase (34). Additional genetic studies indicated that ApbC has a degree of functional redundancy with IscU, a known [Fe-S] cluster scaffolding protein (35,36).In this study we investigate the correlation between the biochemical properties of ApbC (i.e. ATPase activity, [Fe-S] cluster binding, and [Fe-S] cluster transfer rates) and the in vivo function of this protein. This is the first detailed kinetic analysis of ATP hydrolysis for a member of the ParA subfamily of deviant Walker A proteins and the first functional analysis of a member of the ever expanding family of ApbC/Nbp35 proteins. Data presented indicate that noncomplementing variants have distinct biochemical properties that place them in three distinct classes.

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“…Some nitrogen-fixing cyanobacteria such as Nodularia spumigena encode an NfuB protein whose gene is usually clustered with Ni-Fe hydrogenase structural genes. NfuB contains an extra N-terminal domain of unknown function and a C-terminal Rieske domain (24). In humans, alternative splicing of pre-mRNA results in the translation of eukaryotic mitochondrial, cytosolic and nuclear Nfu proteins, all of which comprise a unique N-terminal domain (25).…”

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confidence: 99%

Arabidopsis thaliana Nfu2 Accommodates [2Fe-2S] or [4Fe-4S] Clusters and Is Competent for in Vitro Maturation of Chloroplast [2Fe-2S] and [4Fe-4S] Cluster-Containing Proteins

et al. 2013

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Nfu-type proteins are essential in the biogenesis of iron-sulfur (Fe-S) clusters in numerous organisms. A number of phenotypes including low levels of Fe-S cluster incorporation are associated with deletion of the gene encoding a chloroplast-specific Nfu-type protein, Nfu2 from Arabidopsis thaliana (AtNfu2). Here we report that recombinant AtNfu2 is able to assemble both [2Fe-2S] and [4Fe-4S] clusters. Analytical data and gel filtration studies support cluster/protein stoichiometries of one [2Fe-2S] cluster/homotetramer and one [4Fe-4S] cluster/homodimer. The combination of UV-visible absorption and circular dichroism, resonance Raman and Mössbauer spectroscopies has been employed to investigate the nature, properties and transfer of the clusters assembled on Nfu2. The results are consistent with subunit-bridging [2Fe-2S]2+ and [4Fe-4S]2+ clusters coordinated by the cysteines in the conserved CXXC motif. The results also provided insight into the specificity of Nfu2 for maturation of chloroplastic Fe-S proteins via intact, rapid and quantitative cluster transfer. [2Fe-2S] cluster-bound Nfu2 is shown to be an effective [2Fe-2S]2+ cluster donor for glutaredoxin S16, but not glutaredoxin S14. Moreover, [4Fe-4S] cluster-bound Nfu2 is shown to be a very rapid and efficient [4Fe-4S]2+ cluster donor for adenosine 5′-phosphosulfate reductase (APR1) and yeast two-hybrid studies indicate that APR1 forms a complex with Nfu2, but not with Nfu1 and Nfu3, the two other chloroplastic Nfu proteins. This cluster transfer is likely to be physiologically relevant and is particularly significant for plant metabolism as APR1 catalyzes the second step in reductive sulfur assimilation which ultimately results in the biosynthesis of cysteine, methionine, glutathione, and Fe-S clusters.

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Biogenesis of Iron-Sulfur Clusters in Photosystem I

Cited by 37 publications

References 44 publications

Recent advances in the Suf Fe–S cluster biogenesis pathway: Beyond the Proteobacteria

Recent advances in the Suf Fe–S cluster biogenesis pathway: Beyond the Proteobacteria

Bacterial ApbC Protein Has Two Biochemical Activities That Are Required for in Vivo Function

Arabidopsis thaliana Nfu2 Accommodates [2Fe-2S] or [4Fe-4S] Clusters and Is Competent for in Vitro Maturation of Chloroplast [2Fe-2S] and [4Fe-4S] Cluster-Containing Proteins

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