FeS clusters are prosthetic groups present in all organisms. Proteins with FeS centers are involved in most cellular processes. ISC and SUF are machineries necessary for the formation and insertion of FeS in proteins. Recently, a phylogenetic analysis on more than 10,000 genomes of prokaryotes have uncovered two new systems, MIS and SMS, which were proposed to be ancestral to ISC and SUF. SMS is composed of SmsBC, two homologs of SufBC(D), the scaffolding complex of SUF. In this review, we will specifically focus on the current knowledge of the SUF system and on the new perspectives given by the recent discovery of its ancestor, the SMS system.
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http://dx.doi.org/10.1016/j.bbamcr.2024.119772 | DOI Listing |
Proc Natl Acad Sci U S A
November 2024
CNRS, Aix-Marseille Université, Laboratoire de Chimie Bactérienne, UMR7283, Institut de Microbiologie de la Méditérannée, Institut Microbiologie, Bioénergies et Biotechnologie, Marseille F-13009, France.
Fe-S clusters are essential cofactors involved in many reactions across all domains of life. Their biogenesis in and other enterobacteria involves two machineries: Isc and Suf. Under conditions where cells operate with the Suf system, such as during oxidative stress or iron limitation, the entry of aminoglycosides is reduced, leading to resistance to these antibiotics.
View Article and Find Full Text PDFRSC Chem Biol
September 2024
Institute of Biochemistry and Biology, Department of Molecular Enzymology, University of Potsdam D-14476 Potsdam Germany +49-331-977-5128 +49-331-977-5603.
CyaY, the frataxin homolog of , plays an important role in ISC iron-sulfur cluster assembly through interactions with the cysteine desulfurase IscS, which regulate the supply of sulfur. IscS is not exclusive for ISC Fe-S cluster assembly, as it functions as a hub for the supply of sulfur to a number of other sulfur-requiring pathways, such as for the biosynthesis of Moco and thiolated tRNAs. How the balance of sulfur supply to the various competing pathways is achieved is not fully understood, but a network of protein-protein interactions plays a key role.
View Article and Find Full Text PDFmBio
November 2024
Department of Science, Roma Tre University, Rome, Italy.
Curr Biol
September 2024
Department of Parasitology, Faculty of Science, Charles University, BIOCEV, Průmyslová 595, 25250 Vestec, Czech Republic. Electronic address:
Monocercomonoides exilis is the first known amitochondriate eukaryote. Loss of mitochondria in M. exilis ocurred after the replacement of the essential mitochondrial iron-sulfur cluster (ISC) assembly machinery by a unique, bacteria-derived, cytosolic SUF system.
View Article and Find Full Text PDFJ Biol Chem
August 2024
Department of Chemistry and Biochemistry, University of South Carolina, Columbia, South Carolina, USA. Electronic address:
Iron-sulfur (Fe-S) clusters are required for essential biological pathways, including respiration and isoprenoid biosynthesis. Complex Fe-S cluster biogenesis systems have evolved to maintain an adequate supply of this critical protein cofactor. In Escherichia coli, two Fe-S biosynthetic systems, the "housekeeping" Isc and "stress responsive" Suf pathways, interface with a network of cluster trafficking proteins, such as ErpA, IscA, SufA, and NfuA.
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