Making iron-sulfur cluster: structure, regulation and evolution of the bacterial ISC system

Baussier, Corentin; Fakroun, Soufyan; Aubert, Corinne; Dubrac, Sarah; Mandin, Pierre; Py, Béatrice; Barras, Frédéric

doi:10.1016/bs.ampbs.2020.01.001

Cited by 39 publications

(25 citation statements)

References 178 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…7 ). These features of HybG are reminiscent of the role of the IscA/SufA carrier protein family in iron-sulfur cluster assembly 32 – 34 . In the case of hydrogenase maturation, the HybG–HypD complex is supplied with CN − ligands, originating from carbamoylphosphate 35 , and these ligands are generated and provided by two further accessory proteins HypE and HypF 31 , 36 .…”

Section: Discussionmentioning

confidence: 99%

Native mass spectrometry identifies the HybG chaperone as carrier of the Fe(CN)2CO group during maturation of E. coli [NiFe]-hydrogenase 2

Arlt

Nutschan

Haase

et al. 2021

Sci Rep

View full text Add to dashboard Cite

Abstract[NiFe]-hydrogenases activate dihydrogen. Like all [NiFe]-hydrogenases, hydrogenase 2 of Escherichia coli has a bimetallic NiFe(CN)2CO cofactor in its catalytic subunit. Biosynthesis of the Fe(CN)2CO group of the [NiFe]-cofactor occurs on a distinct scaffold complex comprising the HybG and HypD accessory proteins. HybG is a member of the HypC-family of chaperones that confers specificity towards immature hydrogenase catalytic subunits during transfer of the Fe(CN)2CO group. Using native mass spectrometry of an anaerobically isolated HybG–HypD complex we show that HybG carries the Fe(CN)2CO group. Our results also reveal that only HybG, but not HypD, interacts with the apo-form of the catalytic subunit. Finally, HybG was shown to have two distinct, and apparently CO2-related, covalent modifications that depended on the presence of the N-terminal cysteine residue on the protein, possibly representing intermediates during Fe(CN)2CO group biosynthesis. Together, these findings suggest that the HybG chaperone is involved in both biosynthesis and delivery of the Fe(CN)2CO group to its target protein. HybG is thus suggested to shuttle between the assembly complex and the apo-catalytic subunit. This study provides new insights into our understanding of how organometallic cofactor components are assembled on a scaffold complex and transferred to their client proteins.

show abstract

Section: Discussionmentioning

confidence: 99%

Native mass spectrometry identifies the HybG chaperone as carrier of the Fe(CN)2CO group during maturation of E. coli [NiFe]-hydrogenase 2

Arlt

Nutschan

Haase

et al. 2021

Sci Rep

View full text Add to dashboard Cite

show abstract

“…In the ISC system, class I cysteine desulfurase and sulfur transferase catalyze the pyridoxal 5'‐phosphate (PLP)‐dependent conversion of L‐cysteine to generate the persulfide species and then deliver it to the IscU‐type scaffold (Lill & Freibert, 2020; Braymer et al , 2021). Once the iron and electrons are available, the core ISC complex and the late‐acting ISC machinery accomplish the building and targeting of the [2Fe–2S] and [4Fe–4S] clusters (Melber et al , 2016; Puglisi & Pastore, 2018; Gervason et al , 2019; Patra & Barondeau, 2019; Baussier et al , 2020; Lill & Freibert, 2020; Weiler et al , 2020). Additionally, the ISC components also export a sulfur‐containing factor (X–S) to the cytosol for the CIA machinery (Lill et al , 2015; Ciofi‐Baffoni et al , 2018; Pandey et al , 2018, 2019; Kassube & Thomä, 2020; Lill & Freibert, 2020; Braymer et al , 2021).…”

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

View full text Add to dashboard Cite

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.

show abstract

“…Nature responded by evolving tightly controlled enzymatic pathways that protect Fe-S clusters during their assembly; the complexity of these biosynthetic pathways extended to downstream delivery events too, all of which are tightly regulated. Prokaryotes utilize three different bioassembly pathways to produce Fe-S clusters, including the nitrogen fixation pathway (NIF), the sulfur mobilization pathway (SUF) and the iron-sulfur cluster (ISC) assembly pathway [8][9][10]. Most prokaryotes utilize either the SUF or ISC pathways, but utilization of multiple pathways is often observed.…”

Section: Introductionmentioning

confidence: 99%

Molecular Details of the Frataxin–Scaffold Interaction during Mitochondrial Fe–S Cluster Assembly

Campbell

Pall

Naik

et al. 2021

IJMS

View full text Add to dashboard Cite

Iron–sulfur clusters are essential to almost every life form and utilized for their unique structural and redox-targeted activities within cells during many cellular pathways. Although there are three different Fe–S cluster assembly pathways in prokaryotes (the NIF, SUF and ISC pathways) and two in eukaryotes (CIA and ISC pathways), the iron–sulfur cluster (ISC) pathway serves as the central mechanism for providing 2Fe–2S clusters, directly and indirectly, throughout the entire cell in eukaryotes. Proteins central to the eukaryotic ISC cluster assembly complex include the cysteine desulfurase, a cysteine desulfurase accessory protein, the acyl carrier protein, the scaffold protein and frataxin (in humans, NFS1, ISD11, ACP, ISCU and FXN, respectively). Recent molecular details of this complex (labeled NIAUF from the first letter from each ISC protein outlined earlier), which exists as a dimeric pentamer, have provided real structural insight into how these partner proteins arrange themselves around the cysteine desulfurase, the core dimer of the (NIAUF)2 complex. In this review, we focus on both frataxin and the scaffold within the human, fly and yeast model systems to provide a better understanding of the biophysical characteristics of each protein alone and within the FXN/ISCU complex as it exists within the larger NIAUF construct. These details support a complex dynamic interaction between the FXN and ISCU proteins when both are part of the NIAUF complex and this provides additional insight into the coordinated mechanism of Fe–S cluster assembly.

show abstract

Making iron-sulfur cluster: structure, regulation and evolution of the bacterial ISC system

Cited by 39 publications

References 178 publications

Native mass spectrometry identifies the HybG chaperone as carrier of the Fe(CN)2CO group during maturation of E. coli [NiFe]-hydrogenase 2

Native mass spectrometry identifies the HybG chaperone as carrier of the Fe(CN)2CO group during maturation of E. coli [NiFe]-hydrogenase 2

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

Molecular Details of the Frataxin–Scaffold Interaction during Mitochondrial Fe–S Cluster Assembly

Contact Info

Product

Resources

About