Investigating the role(s) of SufT and the domain of unknown function 59 (DUF59) in the maturation of iron–sulfur proteins
- 263 Downloads
Comprehending biology at the molecular and systems levels is predicated upon understanding the functions of proteins. Proteins are typically composed of one or more functional moieties termed domains. Members of Bacteria, Eukarya, and Archaea utilize proteins containing a domain of unknown function (DUF) 59. Proteins requiring iron–sulfur (FeS) clusters containing cofactors are necessary for nearly all organisms making the assembly of functional FeS proteins essential. Recently, studies in eukaryotic and bacterial organisms have shown that proteins containing a DUF59, or those composed solely of DUF59, function in FeS protein maturation and/or intracellular Fe homeostasis. Herein, we review the current literature, discuss potential roles for DUF59, and address future studies that will help advance the field.
KeywordsIron Sulfur FeS Cluster DUF59 SufT Suf CIA2
The Boyd lab is supported by Rutgers University, the Charles and Johanna Busch foundation, and USDA MRF project NE-1028. A.A.M. is supported by the Douglas Eveleigh fellowship from the Microbial Biology Graduate Program and an Excellence Fellowship from Rutgers University. We thank Hassan Al-Tameemi for his careful reading of the manuscript.
- Gupta V, Sendra M, Naik SG, Chahal HK, Huynh BH, Outten FW, Fontecave M, Ollagnier de Choudens S (2009) Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe–2S] protein and acts as an Fe–S transporter to Fe–S target enzymes. J Am Chem Soc 131:6149–6153CrossRefPubMedPubMedCentralGoogle Scholar
- Lill R, Dutkiewicz R, Freibert SA, Heidenreich T, Mascarenhas J, Netz DJ, Paul VD, Pierik AJ, Richter N, Stumpfig M, Srinivasan V, Stehling O, Muhlenhoff U (2015) The role of mitochondria and the CIA machinery in the maturation of cytosolic and nuclear iron–sulfur proteins. Eur J Cell Biol 94:280–291. doi: 10.1016/j.ejcb.2015.05.002 CrossRefPubMedGoogle Scholar
- Loiseau L, Gerez C, Bekker M, Ollagnier-de Choudens S, Py B, Sanakis Y, Teixeira de Mattos J, Fontecave M, Barras F (2007) ErpA, an iron–sulfur (Fe–S) protein of the A-type essential for respiratory metabolism in Escherichia coli. Proc Natl Acad Sci USA 104:13626–13631CrossRefPubMedPubMedCentralGoogle Scholar
- Mashruwala AA, Pang YY, Rosario-Cruz Z, Chahal HK, Benson MA, Mike LA, Skaar EP, Torres VJ, Nauseef WM, Boyd JM (2015) Nfu facilitates the maturation of iron–sulfur proteins and participates in virulence in Staphylococcus aureus. Mol Microbiol 95:383–409. doi: 10.1111/mmi.12860 CrossRefPubMedGoogle Scholar
- Mashruwala AA, Bhatt S, Poudel S, Boyd ES, Boyd JM (2016a) The DUF59 containing protein SufT is involved in the maturation of iron–sulfur (FeS) proteins during conditions of high FeS cofactor demand in Staphylococcus aureus. PLoS Genet 12:e1006233. doi: 10.1371/journal.pgen.1006233 CrossRefPubMedPubMedCentralGoogle Scholar
- Olivera ER, Minambres B, Garcia B, Muniz C, Moreno MA, Ferrandez A, Diaz E, Garcia JL, Luengo JM (1998) Molecular characterization of the phenylacetic acid catabolic pathway in Pseudomonas putida U: the phenylacetyl-CoA catabolon. Proc Natl Acad Sci USA 95:6419–6424CrossRefPubMedPubMedCentralGoogle Scholar
- Roberts CA, Al-Tameemi HM, Mashruwala AA, Rosario-Cruz Z, Chauhan U, Sause WE, Torres VJ, Belden WJ, Boyd JM (2017) The Suf iron–sulfur cluster biosynthetic system is essential in Staphylococcus aureus and decreased Suf function results in global metabolic defects and reduced survival in human neutrophils. Infect Immun. doi: 10.1128/IAI.00100-17 Google Scholar
- Sheftel AD, Stehling O, Pierik AJ, Elsasser HP, Muhlenhoff U, Webert H, Hobler A, Hannemann F, Bernhardt R, Lill R (2010) Humans possess two mitochondrial ferredoxins, Fdx1 and Fdx2, with distinct roles in steroidogenesis, heme, and Fe/S cluster biosynthesis. Proc Natl Acad Sci USA 107:11775–11780. doi: 10.1073/pnas.1004250107 CrossRefPubMedPubMedCentralGoogle Scholar
- Stehling O, Mascarenhas J, Vashisht AA, Sheftel AD, Niggemeyer B, Rosser R, Pierik AJ, Wohlschlegel JA, Lill R (2013) Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and maturation of different subsets of cytosolic-nuclear iron–sulfur proteins. Cell Metab 18:187–198. doi: 10.1016/j.cmet.2013.06.015 CrossRefPubMedPubMedCentralGoogle Scholar
- Waller JC, Alvarez S, Naponelli V, Lara-Nunez A, Blaby IK, Da Silva V, Ziemak MJ, Vickers TJ, Beverley SM, Edison AS, Rocca JR, Gregory JF 3rd, de Crecy-Lagard V, Hanson AD (2010) A role for tetrahydrofolates in the metabolism of iron–sulfur clusters in all domains of life. Proc Natl Acad Sci USA 107:10412–10417CrossRefPubMedPubMedCentralGoogle Scholar