Iron–Sulfur Cluster Biogenesis in Archaea and Bacteria

Chahal, Harsimranjit K.; Boyd, Jeff M.; Outten, F. Wayne

doi:10.1002/9781119951438.eibc2149

Cited by 3 publications

(8 citation statements)

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“…In early 1990s, the ISC and SUF machineries were identified as the general providers of Fe-S clusters in most organisms, with the exception of some non-nitrogen fixing bacteria that lack the ISC and SUF machineries, in which the NIF machinery is the general source of Fe-S clusters [5,6,8,9,[41][42][43][44][45][46]. Genome wide analysis show that the occurrence of the SUF system is much higher than the ISC one in bacteria and archaea, thus that the SUF system is the housekeeping assembly machinery in these organisms [47].…”

Section: Overview Of the Fe-s Cluster Assembly Machineriesmentioning

confidence: 99%

“…The persulfide of ISCU is reduced by FDX2, possibly into a mononuclear iron-sulfide intermediate (4). Then NFS1 in its open conformation enables the dimerization of ISCU, which leads to formation of a bridged [2Fe2S] cluster in ISCU (5). The bridged [2Fe2S] cluster segregates on one subunit (6) and is transferred to client proteins by the HSC20/HSPA9 chaperone system while a ferrous iron is inserted into apo-ISCU (7).…”

Section: Figurementioning

confidence: 99%

“…Fe-S clusters then became integral part of living organisms to fulfil a wide range of biochemical reactions [4]. The use of Fe-S clusters by living organisms is now widespread among the prokaryotic, archaeal and eukaryotic worlds [5][6][7][8][9]. Even viruses use Fe-S proteins for their replication [10][11][12].…”

Section: Introductionmentioning

confidence: 99%

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Mechanism of Iron–Sulfur Cluster Assembly: In the Intimacy of Iron and Sulfur Encounter

et al. 2020

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Iron–sulfur (Fe–S) clusters are protein cofactors of a multitude of enzymes performing essential biological functions. Specialized multi-protein machineries present in all types of organisms support their biosynthesis. These machineries encompass a scaffold protein on which Fe–S clusters are assembled and a cysteine desulfurase that provides sulfur in the form of a persulfide. The sulfide ions are produced by reductive cleavage of the persulfide, which involves specific reductase systems. Several other components are required for Fe–S biosynthesis, including frataxin, a key protein of controversial function and accessory components for insertion of Fe–S clusters in client proteins. Fe–S cluster biosynthesis is thought to rely on concerted and carefully orchestrated processes. However, the elucidation of the mechanisms of their assembly has remained a challenging task due to the biochemical versatility of iron and sulfur and the relative instability of Fe–S clusters. Nonetheless, significant progresses have been achieved in the past years, using biochemical, spectroscopic and structural approaches with reconstituted system in vitro. In this paper, we review the most recent advances on the mechanism of assembly for the founding member of the Fe–S cluster family, the [2Fe2S] cluster that is the building block of all other Fe–S clusters. The aim is to provide a survey of the mechanisms of iron and sulfur insertion in the scaffold proteins by examining how these processes are coordinated, how sulfide is produced and how the dinuclear [2Fe2S] cluster is formed, keeping in mind the question of the physiological relevance of the reconstituted systems. We also cover the latest outcomes on the functional role of the controversial frataxin protein in Fe–S cluster biosynthesis.

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Section: Overview Of the Fe-s Cluster Assembly Machineriesmentioning

confidence: 99%

Section: Figurementioning

confidence: 99%

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Mechanism of Iron–Sulfur Cluster Assembly: In the Intimacy of Iron and Sulfur Encounter

et al. 2020

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“…Fe-S cofactors are utilized in several molecular functions such as electron transfer and activation of substrates to sense ROS. A family of metalloproteases containing Fe-S cluster takes part in vital cellular functions including ribosome function, amino acid and C metabolism, and transcription [ 99 ]. To assemble these clusters, bacteria employ Fe-S cluster biogenesis systems, such as the iron-sulfur cluster (ISC) pathway.…”

Section: Discussionmentioning

confidence: 99%

“…Although the genes in isc cluster were found to be down-regulated (except iscX ), only hscA and fdx were identified as significantly DEGs in our study. While HscA (and its co-chaperon HscB; FXO12_24270) is involved in ISC assembly or transfer [ 101 ], Fdx acts as an electron donor in the ISC biogenesis pathway [ 99 ]. Two other putative fdx -like genes (FXO12_11905 and FXO12_19935) and an iron-trafficking CyaY protein that supplies iron for ISC biogenesis were also less-expressed under iron-limitation.…”

Section: Discussionmentioning

confidence: 99%

A Novel Marine Pathogen Isolated from Wild Cunners (Tautogolabrus adspersus): Comparative Genomics and Transcriptome Profiling of Pseudomonas sp. Strain J380

et al. 2021

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Cunner (Tautogolabrus adspersus) is a cleaner fish being considered for utilized in the North Atlantic salmon (Salmo salar) aquaculture industry to biocontrol sea lice infestations. However, bacterial diseases due to natural infections in wild cunners have yet to be described. This study reports the isolation of Pseudomonas sp. J380 from infected wild cunners and its phenotypic, genomic, and transcriptomic characterization. This Gram-negative motile rod-shaped bacterium showed a mesophilic (4–28 °C) and halotolerant growth. Under iron-limited conditions, Pseudomonas sp. J380 produced pyoverdine-type fluorescent siderophore. Koch’s postulates were verified in wild cunners by intraperitoneally (i.p.) injecting Pseudomonas sp. J380 at 4 × 103, 4 × 105, and 4 × 107 colony forming units (CFU)/dose. Host-range and comparative virulence were also investigated in lumpfish and Atlantic salmon i.p. injected with ~106 CFU/dose. Lumpfish were more susceptible compared to cunners, and Atlantic salmon was resistant to Pseudomonas sp. J380 infection. Cunner tissues were heavily colonized by Pseudomonas sp. J380 compared to lumpfish and Atlantic salmon suggesting that it might be an opportunistic pathogen in cunners. The genome of Pseudomonas sp. J380 was 6.26 megabases (Mb) with a guanine-cytosine (GC) content of 59.7%. Biochemical profiles, as well as comparative and phylogenomic analyses, suggested that Pseudomonas sp. J380 belongs to the P. fluorescens species complex. Transcriptome profiling under iron-limited vs. iron-enriched conditions identified 1159 differentially expressed genes (DEGs). Cellular metabolic processes, such as ribosomal and energy production, and protein synthesis, were impeded by iron limitation. In contrast, genes involved in environmental adaptation mechanisms including two-component systems, histidine catabolism, and redox balance were transcriptionally up-regulated. Furthermore, iron limitation triggered the differential expression of genes encoding proteins associated with iron homeostasis. As the first report on a bacterial infection in cunners, the current study provides an overview of a new marine pathogen, Pseudomonas sp. J380.

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Iron Insertion at the Assembly Site of the ISCU Scaffold Protein Is a Conserved Process Initiating Fe–S Cluster Biosynthesis

et al. 2022

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Iron–sulfur (Fe–S) clusters are prosthetic groups of proteins biosynthesized on scaffold proteins by highly conserved multi-protein machineries. Biosynthesis of Fe–S clusters into the ISCU scaffold protein is initiated by ferrous iron insertion, followed by sulfur acquisition, via a still elusive mechanism. Notably, whether iron initially binds to the ISCU cysteine-rich assembly site or to a cysteine-less auxiliary site via N/O ligands remains unclear. We show here by SEC, circular dichroism (CD), and Mössbauer spectroscopies that iron binds to the assembly site of the monomeric form of prokaryotic and eukaryotic ISCU proteins via either one or two cysteines, referred to the 1-Cys and 2-Cys forms, respectively. The latter predominated at pH 8.0 and correlated with the Fe–S cluster assembly activity, whereas the former increased at a more acidic pH, together with free iron, suggesting that it constitutes an intermediate of the iron insertion process. Iron not binding to the assembly site was non-specifically bound to the aggregated ISCU, ruling out the existence of a structurally defined auxiliary site in ISCU. Characterization of the 2-Cys form by site-directed mutagenesis, CD, NMR, X-ray absorption, Mössbauer, and electron paramagnetic resonance spectroscopies showed that the iron center is coordinated by four strictly conserved amino acids of the assembly site, Cys35, Asp37, Cys61, and His103, in a tetrahedral geometry. The sulfur receptor Cys104 was at a very close distance and apparently bound to the iron center when His103 was missing, which may enable iron-dependent sulfur acquisition. Altogether, these data provide the structural basis to elucidate the Fe–S cluster assembly process and establish that the initiation of Fe–S cluster biosynthesis by insertion of a ferrous iron in the assembly site of ISCU is a conserved mechanism.

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Iron–Sulfur Cluster Biogenesis in Archaea and Bacteria

Cited by 3 publications

References 226 publications

Mechanism of Iron–Sulfur Cluster Assembly: In the Intimacy of Iron and Sulfur Encounter

Mechanism of Iron–Sulfur Cluster Assembly: In the Intimacy of Iron and Sulfur Encounter

A Novel Marine Pathogen Isolated from Wild Cunners (Tautogolabrus adspersus): Comparative Genomics and Transcriptome Profiling of Pseudomonas sp. Strain J380

Iron Insertion at the Assembly Site of the ISCU Scaffold Protein Is a Conserved Process Initiating Fe–S Cluster Biosynthesis

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