Fe-S cluster biogenesis by the bacterial Suf pathway

Blahut, Matthew; Sanchez, Enis; Fisher, Claire E.; Outten, F. Wayne

doi:10.1016/j.bbamcr.2020.118829

Cited by 55 publications

(42 citation statements)

References 80 publications

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“…In the SUF system, a persulfide is generated by a class II cysteine desulfurase (bacterial SufS or plant NFS2) with the activation from sulfur transferase (bacterial SufE or plant SUFE1‐3) and then transferred to the SufBCD scaffold complex (Balk & Schaedler, 2014; Pérard & Ollagnier de Choudens, 2018; Blahut et al , 2019; Braymer et al , 2021). In the presence of iron and electrons, the newly made Fe–S cluster is assembled on the SUFB/D dimer interface with ATP hydrolysis catalyzed by the ABC‐type ATPase SUFC subunit and is then released and delivered to apo‐proteins through various carrier proteins, such as A‐type carriers (bacterial SufA or plant SUFA), NifU‐like proteins (bacterial NfuA or chloroplast NFUs), glutaredoxins (plant GRX14/16), and plant HCF101 (Balk & Schaedler, 2014; Hirabayashi et al , 2015; Hu et al , 2017; Yuda et al , 2017; Przybyla‐Toscano et al , 2018; Garcia et al , 2019; Berger et al , 2020; Blahut et al , 2020; Roland et al , 2020).…”

Section: Introductionmentioning

confidence: 99%

The DnaJ proteins DJA6 and DJA5 are essential for chloroplast iron–sulfur cluster biogenesis

Bai

Ouyang

et al. 2021

The EMBO Journal

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Fe–S clusters are ancient, ubiquitous and highly essential prosthetic groups for numerous fundamental processes of life. The biogenesis of Fe–S clusters is a multistep process including iron acquisition, sulfur mobilization, and cluster formation. Extensive studies have provided deep insights into the mechanism of the latter two assembly steps. However, the mechanism of iron utilization during chloroplast Fe–S cluster biogenesis is still unknown. Here we identified two Arabidopsis DnaJ proteins, DJA6 and DJA5, that can bind iron through their conserved cysteine residues and facilitate iron incorporation into Fe–S clusters by interactions with the SUF (sulfur utilization factor) apparatus through their J domain. Loss of these two proteins causes severe defects in the accumulation of chloroplast Fe–S proteins, a dysfunction of photosynthesis, and a significant intracellular iron overload. Evolutionary analyses revealed that DJA6 and DJA5 are highly conserved in photosynthetic organisms ranging from cyanobacteria to higher plants and share a strong evolutionary relationship with SUFE1, SUFC, and SUFD throughout the green lineage. Thus, our work uncovers a conserved mechanism of iron utilization for chloroplast Fe–S cluster biogenesis.

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Section: Introductionmentioning

confidence: 99%

The DnaJ proteins DJA6 and DJA5 are essential for chloroplast iron–sulfur cluster biogenesis

Bai

Ouyang

et al. 2021

The EMBO Journal

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“…Fe-S complexes are metal cofactors required for the function of a variety of essential processes (e.g. respiration and DNA repair) and can be assembled by E. coli via either the iron-sulfur cluster (ISC) or the sulfur formation (SUF) pathways [ 41 ]. The SUF pathway in E. coli is associated with Fe-S cluster assembly during iron deficiency or oxidative stress [ 41 ].…”

Section: Discussionmentioning

confidence: 99%

“…respiration and DNA repair) and can be assembled by E. coli via either the iron-sulfur cluster (ISC) or the sulfur formation (SUF) pathways [ 41 ]. The SUF pathway in E. coli is associated with Fe-S cluster assembly during iron deficiency or oxidative stress [ 41 ]. Upon treatment with Atr-DEF2(G39-C54), cysteine desulfurase SufS (Q8FH54, FC: 3.0), Fe-S cluster assembly protein SufD (A0A0H2V7L8, FC: 4.3), probable ATP-dependent transporter SufC (A0A0H2V7V5, FC: 4.2), and Fe-S cluster assembly protein SufB (A0A0H2V9X7, FC: 6.2) showed increased abundance (Fig.…”

Section: Discussionmentioning

confidence: 99%

Proteomic response of Escherichia coli to a membrane lytic and iron chelating truncated Amaranthus tricolor defensin

et al. 2021

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Background Plant defensins are a broadly distributed family of antimicrobial peptides which have been primarily studied for agriculturally relevant antifungal activity. Recent studies have probed defensins against Gram-negative bacteria revealing evidence for multiple mechanisms of action including membrane lysis and ribosomal inhibition. Herein, a truncated synthetic analog containing the γ-core motif of Amaranthus tricolor DEF2 (Atr-DEF2) reveals Gram-negative antibacterial activity and its mechanism of action is probed via proteomics, outer membrane permeability studies, and iron reduction/chelation assays. Results Atr-DEF2(G39-C54) demonstrated activity against two Gram-negative human bacterial pathogens, Escherichia coli and Klebsiella pneumoniae. Quantitative proteomics revealed changes in the E. coli proteome in response to treatment of sub-lethal concentrations of the truncated defensin, including bacterial outer membrane (OM) and iron acquisition/processing related proteins. Modification of OM charge is a common response of Gram-negative bacteria to membrane lytic antimicrobial peptides (AMPs) to reduce electrostatic interactions, and this mechanism of action was confirmed for Atr-DEF2(G39-C54) via an N-phenylnaphthalen-1-amine uptake assay. Additionally, in vitro assays confirmed the capacity of Atr-DEF2(G39-C54) to reduce Fe3+ and chelate Fe2+ at cell culture relevant concentrations, thus limiting the availability of essential enzymatic cofactors. Conclusions This study highlights the utility of plant defensin γ-core motif synthetic analogs for characterization of novel defensin activity. Proteomic changes in E. coli after treatment with Atr-DEF2(G39-C54) supported the hypothesis that membrane lysis is an important component of γ-core motif mediated antibacterial activity but also emphasized that other properties, such as metal sequestration, may contribute to a multifaceted mechanism of action.

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“…Life in aerobiosis apparently led to its complexification, notably adding the SufA / D / E / S genes to the “ancestral” SufB / C genes as it now exists in the E. coli SUF operon (SufABCDSE) [ 12 ]. In this model bacterium, the SUF machinery operates under stress and Fe starvation conditions when the housekeeping ISC (iron-sulfur cluster) machinery is no longer operative [ 11 , 16 ]. However, in some other bacteria, the SUF system is the sole or major Fe-S biogenesis system, with some genes such as SufD sometimes being absent, or new ones such as SufU or SufT having appeared [ 15 ].…”

Section: Maturation Of Iron-sulfur Proteins By the Suf Machinerymentioning

confidence: 99%

Occurrence, Evolution and Specificities of Iron-Sulfur Proteins and Maturation Factors in Chloroplasts from Algae

Przybyla-Toscano

Couturier

Remacle

et al. 2021

IJMS

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Iron-containing proteins, including iron-sulfur (Fe-S) proteins, are essential for numerous electron transfer and metabolic reactions. They are present in most subcellular compartments. In plastids, in addition to sustaining the linear and cyclic photosynthetic electron transfer chains, Fe-S proteins participate in carbon, nitrogen, and sulfur assimilation, tetrapyrrole and isoprenoid metabolism, and lipoic acid and thiamine synthesis. The synthesis of Fe-S clusters, their trafficking, and their insertion into chloroplastic proteins necessitate the so-called sulfur mobilization (SUF) protein machinery. In the first part, we describe the molecular mechanisms that allow Fe-S cluster synthesis and insertion into acceptor proteins by the SUF machinery and analyze the occurrence of the SUF components in microalgae, focusing in particular on the green alga Chlamydomonas reinhardtii. In the second part, we describe chloroplastic Fe-S protein-dependent pathways that are specific to Chlamydomonas or for which Chlamydomonas presents specificities compared to terrestrial plants, putting notable emphasis on the contribution of Fe-S proteins to chlorophyll synthesis in the dark and to the fermentative metabolism. The occurrence and evolutionary conservation of these enzymes and pathways have been analyzed in all supergroups of microalgae performing oxygenic photosynthesis.

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Fe-S cluster biogenesis by the bacterial Suf pathway

Cited by 55 publications

References 80 publications

The DnaJ proteins DJA6 and DJA5 are essential for chloroplast iron–sulfur cluster biogenesis

The DnaJ proteins DJA6 and DJA5 are essential for chloroplast iron–sulfur cluster biogenesis

Proteomic response of Escherichia coli to a membrane lytic and iron chelating truncated Amaranthus tricolor defensin

Occurrence, Evolution and Specificities of Iron-Sulfur Proteins and Maturation Factors in Chloroplasts from Algae

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