Gene Symbol: sufS
Description: cysteine desulfurase, stimulated by SufE; selenocysteine lyase, PLP-dependent
Alias: ECK1676, JW1670, csdB, ynhB
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Dai Y, Outten F. The E. coli SufS-SufE sulfur transfer system is more resistant to oxidative stress than IscS-IscU. FEBS Lett. 2012;586:4016-22 pubmed publisher
    ..To determine why the Suf pathway is favored under stress conditions, the stress response SufS-SufE sulfur transfer pathway and the basal housekeeping IscS-IscU pathway were directly compared...
  2. Mihara H, Kato S, Lacourciere G, Stadtman T, Kennedy R, Kurihara T, et al. The iscS gene is essential for the biosynthesis of 2-selenouridine in tRNA and the selenocysteine-containing formate dehydrogenase H. Proc Natl Acad Sci U S A. 2002;99:6679-83 pubmed
    Three NifS-like proteins, IscS, CSD, and CsdB, from Escherichia coli catalyze the removal of sulfur and selenium from L-cysteine and L-selenocysteine, respectively, to form L-alanine...
  3. Lacourciere G, Stadtman T. Utilization of selenocysteine as a source of selenium for selenophosphate biosynthesis. Biofactors. 2001;14:69-74 pubmed
    ..Recently, three E. coli NifS-like proteins, CsdB, CSD, and IscS, were characterized...
  4. O Mahony D, Hughes D, Thompson S, Atkins J. Suppression of a -1 frameshift mutation by a recessive tRNA suppressor which causes doublet decoding. J Bacteriol. 1989;171:3824-30 pubmed
    b>sufS was found to suppress the only known suppressible-1 frameshift mutation, trpE91, at a site identified as GGA and mapped within the single gene of the only tRNA that can decode GGA in Escherichia coli...
  5. Prabhakar R, Morokuma K, Musaev D. A comparative study of various computational approaches in calculating the structure of pyridoxal 5'-phosphate (PLP)-dependent beta-lyase protein. The importance of protein environment. J Comput Chem. 2005;26:443-6 pubmed
    ..B3LYP), and various ONIOM methods, have been comparatively investigated for the structure of Escherichia coli NifS CsdB protein...
  6. Fontecave M, Choudens S, Py B, Barras F. Mechanisms of iron-sulfur cluster assembly: the SUF machinery. J Biol Inorg Chem. 2005;10:713-21 pubmed
  7. Mihara H, Maeda M, Fujii T, Kurihara T, Hata Y, Esaki N. A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary x-ray crystallographic studies. J Biol Chem. 1999;274:14768-72 pubmed
    ..An open reading frame, named csdB, from Escherichia coli encodes a putative protein that is similar to selenocysteine lyase of pig liver and cysteine ..
  8. Mihara H, Kurihara T, Yoshimura T, Esaki N. Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions. J Biochem. 2000;127:559-67 pubmed
    We have purified three NifS homologs from Escherichia coli, CSD, CsdB, and IscS, that appear to be involved in iron-sulfur cluster formation and/or the biosynthesis of selenophosphate...
  9. Lima C. Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation. J Mol Biol. 2002;315:1199-208 pubmed
    The Escherichia coli NifS CsdB protein is a member of the homodimeric pyridoxal 5'-phosphate (PLP)-dependent family of enzymes...

More Information


  1. Zheng M, Wang X, Templeton L, Smulski D, LaRossa R, Storz G. DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J Bacteriol. 2001;183:4562-70 pubmed
    ..These results expand our understanding of the oxidative stress response and raise interesting questions regarding the nature of other regulators that modulate gene expression in response to hydrogen peroxide. ..
  2. Sendra M, Ollagnier de Choudens S, Lascoux D, Sanakis Y, Fontecave M. The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from the SUFS-SUFE complex to SUFA. FEBS Lett. 2007;581:1362-8 pubmed
    ..from Escherichia coli, used here as a model scaffold protein is competent for binding sulfur atoms provided by the SufS-SufE cysteine desulfurase system covalently as shown by mass spectrometry...
  3. Lacourciere G, Mihara H, Kurihara T, Esaki N, Stadtman T. Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate. J Biol Chem. 2000;275:23769-73 pubmed
    ..Recently, three E. coli NifS-like proteins, CsdB, CSD, and IscS, have been overexpressed and characterized...
  4. Dai Y, Kim D, Dong G, Busenlehner L, Frantom P, Outten F. SufE D74R Substitution Alters Active Site Loop Dynamics To Further Enhance SufE Interaction with the SufS Cysteine Desulfurase. Biochemistry. 2015;54:4824-33 pubmed publisher
    ..In Escherichia coli, the SufS cysteine desulfurase mobilizes persulfide from l-cysteine via a PLP-dependent ping-pong reaction...
  5. Pagel F, Tuohy T, Atkins J, Murgola E. Doublet translocation at GGA is mediated directly by mutant tRNA(2Gly). J Bacteriol. 1992;174:4179-82 pubmed
    Members of the sufS class of -1 frameshift suppressors have alterations of the GGA/G-decoding tRNA(2Gly). Suppressor-promoted frameshifting at GGA was shown in this study to be directly mediated by the mutant tRNA(2Gly)...
  6. Bühning M, Valleriani A, Leimkuhler S. The Role of SufS Is Restricted to Fe-S Cluster Biosynthesis in Escherichia coli. Biochemistry. 2017;56:1987-2000 pubmed publisher
    ..share a high degree of similarity, we show that the function of their respective l-cysteine desulfurase IscS or SufS is specific for each cellular pathway...
  7. Layer G, Gaddam S, Ayala Castro C, Ollagnier de Choudens S, Lascoux D, Fontecave M, et al. SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly. J Biol Chem. 2007;282:13342-50 pubmed
    ..Here we describe how the SufS and SufE proteins interact with the SufBCD protein complex to facilitate sulfur liberation from cysteine and ..
  8. Lee J, Hiibel S, Reardon K, Wood T. Identification of stress-related proteins in Escherichia coli using the pollutant cis-dichloroethylene. J Appl Microbiol. 2010;108:2088-102 pubmed publisher
    ..using the most hydrogen peroxide-sensitive mutants, ygiW and ychH, identified that FliS, GalS, HcaR, MglA, SufE, SufS, Tap, TnaB, YhcN and YjaA are also involved in the stress response of E...
  9. Rojas D, Vásquez C. Sensitivity to potassium tellurite of Escherichia coli cells deficient in CSD, CsdB and IscS cysteine desulfurases. Res Microbiol. 2005;156:465-71 pubmed
    The csdA, csdB and iscS genes encoding for cysteine desulfurase enzymatic activities in Escherichia coli were independently inactivated and potassium tellurite sensitivity, determined for each of the resulting mutant clones, was found to ..
  10. Tokumoto U, Kitamura S, Fukuyama K, Takahashi Y. Interchangeability and distinct properties of bacterial Fe-S cluster assembly systems: functional replacement of the isc and suf operons in Escherichia coli with the nifSU-like operon from Helicobacter pylori. J Biochem. 2004;136:199-209 pubmed
    ..While the differences between ISC and SUF were small with respect to the complementing activity, the SUF system appears to be more advantageous for bacterial growth in the presence of hydrogen peroxide. ..
  11. Ollagnier de Choudens S, Lascoux D, Loiseau L, Barras F, Forest E, Fontecave M. Mechanistic studies of the SufS-SufE cysteine desulfurase: evidence for sulfur transfer from SufS to SufE. FEBS Lett. 2003;555:263-7 pubmed
    b>SufS is a cysteine desulfurase of the suf operon shown to be involved in iron-sulfur cluster biosynthesis under iron limitation and oxidative stress conditions...
  12. Outten F, Wood M, Munoz F, Storz G. The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J Biol Chem. 2003;278:45713-9 pubmed
    ..To examine the biochemical roles of the Suf proteins, we purified all of the proteins and assayed their effect on SufS cysteine desulfurase activity...
  13. Falahee M, Weiss R, O Connor M, Doonan S, Gesteland R, Atkins J. Mutants of translational components that alter reading frame by two steps forward or one step back. J Biol Chem. 1988;263:18099-103 pubmed
    External suppressors, sufS, of a -1 frameshift mutant cause ribosomes to shift into the -1 frame when reading the sequence CAG GGA GUG. The resulting product is not Gln-Gly-Val but Gln-Gly-Ser with Ser being encoded by the underlined AGU...
  14. Bolstad H, Wood M. An in vivo method for characterization of protein interactions within sulfur trafficking systems of E. coli. J Proteome Res. 2010;9:6740-51 pubmed publisher
    ..We identified SufE-SufS and SufE-SufB interactions, interactions previously demonstrated in vitro, indicating that our method has the ..
  15. Djaman O, Outten F, Imlay J. Repair of oxidized iron-sulfur clusters in Escherichia coli. J Biol Chem. 2004;279:44590-9 pubmed
  16. Lauhon C. Requirement for IscS in biosynthesis of all thionucleosides in Escherichia coli. J Bacteriol. 2002;184:6820-9 pubmed
    ..In addition to iscS, E. coli contains two other nifS homologs, csdA and csdB, each of which has cysteine desulfurase activity and could potentially donate sulfur for thionucleoside ..
  17. Takahashi Y, Tokumoto U. A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J Biol Chem. 2002;277:28380-3 pubmed
    ..The genes homologous to sufBC are present in a wide range of bacteria, Archaea, and plastids, suggesting that this type of system is almost ubiquitous in nature. ..
  18. Mihara H, Fujii T, Kato S, Kurihara T, Hata Y, Esaki N. Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine. J Biochem. 2002;131:679-85 pubmed
    Escherichia coli CsdB is a pyridoxal 5'-phosphate (PLP)-dependent enzyme that catalyzes both cysteine desulfuration and selenocysteine deselenation. The enzyme has a high specific activity for L-selenocysteine relative to L-cysteine...
  19. Leimkuhler S, Rajagopalan K. A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli. J Biol Chem. 2001;276:22024-31 pubmed the presence of a persulfide-containing sulfurtransferase such as IscS, cysteine sulfinate desulfinase (CSD), or CsdB. A fully defined in vitro system has been developed in which an inactive form of MPT synthase can be activated by ..
  20. Ranquet C, Ollagnier de Choudens S, Loiseau L, Barras F, Fontecave M. Cobalt stress in Escherichia coli. The effect on the iron-sulfur proteins. J Biol Chem. 2007;282:30442-51 pubmed
    ..We propose a model wherein cobalt competes out iron during synthesis of [Fe-S] clusters in metabolically essential proteins. ..
  21. Lee K, Yeo W, Roe J. Oxidant-responsive induction of the suf operon, encoding a Fe-S assembly system, through Fur and IscR in Escherichia coli. J Bacteriol. 2008;190:8244-7 pubmed publisher
    ..For apo-IscR to bind, oxidation-mediated dissociation of Fur is required. Therefore, a peroxide-responsive signal is transduced through OxyR, IscR, and Fur to achieve oxidation-sensitive and maximal induction of this operon. ..
  22. Nachin L, El Hassouni M, Loiseau L, Expert D, Barras F. SoxR-dependent response to oxidative stress and virulence of Erwinia chrysanthemi: the key role of SufC, an orphan ABC ATPase. Mol Microbiol. 2001;39:960-72 pubmed
    ..analysis revealed six open reading frames that were homologous to the Escherichia coli sufA, sufB, sufC, sufD, sufS and sufE genes...
  23. Patzer S, Hantke K. SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli. J Bacteriol. 1999;181:3307-9 pubmed
    Escherichia coli fhuF mutants, a sufS::MudI mutant, and a sufD::MudI mutant were found to have the same phenotype: the inability to use ferrioxamine B as an iron source in a plate assay...
  24. Loiseau L, Ollagnier de Choudens S, Nachin L, Fontecave M, Barras F. Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J Biol Chem. 2003;278:38352-9 pubmed publisher
    ..SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no ..
  25. Kurihara T, Mihara H, Kato S, Yoshimura T, Esaki N. Assembly of iron-sulfur clusters mediated by cysteine desulfurases, IscS, CsdB and CSD, from Escherichia coli. Biochim Biophys Acta. 2003;1647:303-9 pubmed
    ..Escherichia coli has three cysteine desulfurases named IscS, CsdB and CSD. We found that each of them facilitates the formation of the iron-sulfur cluster of ferredoxin in vitro...
  26. Fujii T, Maeda M, Mihara H, Kurihara T, Esaki N, Hata Y. Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase. Biochemistry. 2000;39:1263-73 pubmed
    Escherichia coli CsdB, a NifS homologue with a high specificity for L-selenocysteine, is a pyridoxal 5'-phosphate (PLP)-dependent dimeric enzyme that belongs to aminotransferases class V in fold-type I of PLP enzymes and catalyzes the ..