Book Chapter10.1016/BS.AMPBS.2020.01.001
Making iron-sulfur cluster: structure, regulation and evolution of the bacterial ISC system
Corentin Baussier,Soufyan Fakroun,Corinne Aubert,Sarah Dubrac,Pierre Mandin,Béatrice Py,Frédéric Barras +6 more
42
TL;DR: This review aims to highlight Fe-S biogenesis facets remaining matters of discussion, such as the role of frataxin, or the link between fatty acid metabolism andFe-S homeostasis, and discusses recent advances on strategies used by different species to make and use Fe- S clusters in changing redox environmental conditions.
read more
Abstract: Iron sulfur (Fe-S) clusters rank among the most ancient and conserved prosthetic groups. Fe-S clusters containing proteins are present in most, if not all, organisms. Fe-S clusters containing proteins are involved in a wide range of cellular processes, from gene regulation to central metabolism, via gene expression, RNA modification or bioenergetics. Fe-S clusters are built by biogenesis machineries conserved throughout both prokaryotes and eukaryotes. We focus mostly on bacterial ISC machinery, but not exclusively, as we refer to eukaryotic ISC system when it brings significant complementary information. Besides covering the structural and regulatory aspects of Fe-S biogenesis, this review aims to highlight Fe-S biogenesis facets remaining matters of discussion, such as the role of frataxin, or the link between fatty acid metabolism and Fe-S homeostasis. Last, we discuss recent advances on strategies used by different species to make and use Fe-S clusters in changing redox environmental conditions.
read more
Chat with Paper
AI Agents for this Paper
Find similar papers on Google Scholar, PubMed and Arxiv
Write a critical review of this paper
Analyze citations of this paper to find unaddressed research gaps
Citations
Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis (nitrogenase/FeS cores/pyridoxal phosphate/sulfur mobilization/cysteinyl persulfide)
Limin Zheng,Robert H. WHITEt,Valerie L. Cash,Richard F. Jack,Dennis R. Dean +4 more
- 01 Jan 2016
TL;DR: In this paper, it was shown that NIFS is a pyridoxal phosphate-containing homodimer that catalyzes the formation of L-alanine and elemental sulfur by using L-cysteine as substrate.
490
Mechanistic concepts of iron-sulfur protein biogenesis in Biology.
TL;DR: This review provides a comprehensive and comparative overview of the various known biogenesis systems in Biology, and summarizes their common or diverging molecular mechanisms, thereby illustrating both the conservation and diverse adaptions of these four machineries during evolution and under different lifestyles.
177
The DnaJ proteins DJA6 and DJA5 are essential for chloroplast iron–sulfur cluster biogenesis
Jing Zhang,Jing Zhang,Zechen Bai,Min Ouyang,Xiumei Xu,Haibo Xiong,Qiang Wang,Bernhard Grimm,Jean-David Rochaix,Lixin Zhang +9 more
TL;DR: In this paper, the authors 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.
29
Iron Insertion at the Assembly Site of the ISCU Scaffold Protein Is a Conserved Process Initiating Fe-S Cluster Biosynthesis.
B. Srour,Sylvain Gervason,Maren Hellen Hoock,Beata Marta Monfort,K K Want,Djabir Larkem,Nadine Trabelsi,Gautier Landrot,Andrea Zitolo,Emiliano Fonda,Emilien Etienne,Guillaume Gerbaud,Christina S. Müller,Jonathan Oltmanns,Jesse B. Gordon,Vishal Yadav,Malgorzata Kleczewska,Marcin Jelen,Michel B. Toledano,Rafal Dutkiewicz,David P. Goldberg,Volker Schünemann,Bruno Guigliarelli,Bénédicte Burlat,Christina Sizun,Benoît D'Autréaux +25 more
TL;DR: In this article , it was shown that the insertion of a ferrous iron in the assembly site of ISCU proteins is a conserved mechanism and that the iron center is coordinated by four strictly conserved amino acids, i.e., Cys35, Asp37, Cys61, and His103.
26
Influence of erbium doping on zinc oxide nanoparticles: Structural, optical and antimicrobial activity
Angélica Lizeth Sánchez-López,Y. Perfecto-Avalos,A. Sanchez-Martinez,O. Ceballos-Sanchez,M. Sepulveda-Villegas,Gabriel Rincón-Enríquez,Vicente Rodríguez-González,Rebeca García-Varela,L. Marcelo Lozano,Diego Eloyr Navarro-López,Gildardo Sanchez-Ante,Kaled Corona-Romero,Edgar R. López-Mena +12 more
TL;DR: In this paper, the influence of erbium content in structural, optical, and antimicrobial activity of Zn1-xErxO (0, 1, 5, 10 at%) nanoparticles was analyzed.
24
References
Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli.
TL;DR: A model in which the fdx gene product functions as an intermediate site for Fe-S cluster assembly is proposed, which shows the iscS, iscA, hscA, and fdx genes to be required for the assembly of theFe-S clusters.
269
HilD, HilC and RtsA constitute a feed forward loop that controls expression of the SPI1 type three secretion system regulator hilA in Salmonella enterica serovar Typhimurium.
TL;DR: It is shown that ‘SPI1 inducing conditions’ cause independent activation of the rtsA, hilC and hilD genes in the absence of known regulators, which provides a framework for future studies aimed at understanding this complicated regulatory network.
266
Genetic Analysis of the isc Operon in Escherichia coli Involved in the Biogenesis of Cellular Iron-Sulfur Proteins
TL;DR: These findings support the conclusion that IscS, via cysteine desulfurase activity, provides the sulfur that is subsequently incorporated into Fe-S clusters by assembler machinery comprising of the iscUA-hscBA-fdx gene products.
264
IscR‐dependent gene expression links iron‐sulphur cluster assembly to the control of O2‐regulated genes in Escherichia coli
TL;DR: The findings presented here indicate a more general role of IscR in the regulation of Fe‐S cluster biogenesis and that iscR contributes to the O2 regulation of several promoters controlling the expression of anaerobic Fe‐sulphur proteins.
Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones.
TL;DR: Hsp70 chaperones are central hubs of the protein quality control network and collaborate with co-chaperones having a J-domain having a flexible loop and a conserved His–Pro–Asp motif required for ATP hydrolysis by Hsp70s to facilitate many protein-folding processes that (re)establish protein homeostasis.
234