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The cysteine desulfurase IscS of Mycobacterium tuberculosis is involved in iron-sulfur cluster biogenesis and oxidative stress defence.

Rybniker J, Pojer F, Marienhagen J, Kolly GS, Chen JM, van Gumpel E, Hartmann P, Cole ST
Biochem J 459 467-78 (2014)
Cited: 19 times
EuropePMC logo PMID: 24548275

Abstract

The complex multiprotein systems for the assembly of protein-bound iron-sulfur (Fe-S) clusters are well defined in Gram-negative model organisms. However, little is known about Fe-S cluster biogenesis in other bacterial species. The ISC (iron-sulfur cluster) operon of Mycobacterium tuberculosis lacks several genes known to be essential for the function of this system in other organisms. However, the cysteine desulfurase IscSMtb (Rv number Rv3025c; Mtb denotes M. tuberculosis) is conserved in this important pathogen. The present study demonstrates that deleting iscSMtb renders the cells microaerophilic and hypersensitive to oxidative stress. Moreover, the ∆iscSMtb mutant shows impaired Fe-S cluster-dependent enzyme activity, clearly indicating that IscSMtb is associated with Fe-S cluster assembly. An extensive interaction network of IscSMtb with Fe-S proteins was identified, suggesting a novel mechanism of sulfur transfer by direct interaction with apoproteins. Interestingly, the highly homologous IscS of Escherichia coli failed to complement the ∆iscSMtb mutant and showed a less diverse protein-interaction profile. To identify a structural basis for these observations we determined the crystal structure of IscSMtb, which mirrors adaptations made in response to an ISC operon devoid of IscU-like Fe-S cluster scaffold proteins. We conclude that in M. tuberculosis IscS has been redesigned during evolution to compensate for the deletion of large parts of the ISC operon.

Articles - 4isy mentioned but not cited (1)

  1. Structural evidence for a latch mechanism regulating access to the active site of SufS-family cysteine desulfurases. Dunkle JA, Bruno MR, Frantom PA. Acta Crystallogr D Struct Biol 76 291-301 (2020)


Reviews citing this publication (4)

  1. Chemistry and Redox Biology of Mycothiol. Reyes AM, Pedre B, De Armas MI, Tossounian MA, Radi R, Messens J, Trujillo M. Antioxid Redox Signal 28 487-504 (2018)
  2. The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis. Das M, Dewan A, Shee S, Singh A. Antioxidants (Basel) 10 997 (2021)
  3. Improved understanding of pathogenesis from protein interactions in Mycobacterium tuberculosis. Cui T, He ZG. Expert Rev Proteomics 11 745-755 (2014)
  4. Survival in Hostile Conditions: Pupylation and the Proteasome in Actinobacterial Stress Response Pathways. von Rosen T, Keller LM, Weber-Ban E. Front Mol Biosci 8 685757 (2021)

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  1. Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex. Boniecki MT, Freibert SA, Mühlenhoff U, Lill R, Cygler M. Nat Commun 8 1287 (2017)
  2. SufB intein of Mycobacterium tuberculosis as a sensor for oxidative and nitrosative stresses. Topilina NI, Green CM, Jayachandran P, Kelley DS, Stanger MJ, Piazza CL, Nayak S, Belfort M. Proc Natl Acad Sci U S A 112 10348-10353 (2015)
  3. Rv1460, a SufR homologue, is a repressor of the suf operon in Mycobacterium tuberculosis. Willemse D, Weber B, Masino L, Warren RM, Adinolfi S, Pastore A, Williams MJ. PLoS One 13 e0200145 (2018)
  4. Cysteine Desulfurase IscS2 Plays a Role in Oxygen Resistance in Clostridium difficile. Giordano N, Hastie JL, Smith AD, Foss ED, Gutierrez-Munoz DF, Carlson PE. Infect Immun 86 e00326-18 (2018)
  5. Comparative Proteomics and Secretomics Revealed Virulence and Antibiotic Resistance-Associated Factors in Vibrio parahaemolyticus Recovered From Commonly Consumed Aquatic Products. Zhu Z, Yang L, Yu P, Wang Y, Peng X, Chen L. Front Microbiol 11 1453 (2020)
  6. Mycobacterium tuberculosis SufR responds to nitric oxide via its 4Fe-4S cluster and regulates Fe-S cluster biogenesis for persistence in mice. Anand K, Tripathi A, Shukla K, Malhotra N, Jamithireddy AK, Jha RK, Chaudhury SN, Rajmani RS, Ramesh A, Nagaraja V, Gopal B, Nagaraju G, Narain Seshayee AS, Singh A. Redox Biol 46 102062 (2021)
  7. Structural Analysis of an l-Cysteine Desulfurase from an Ssp DNA Phosphorothioation System. Liu L, Jiang S, Xing M, Chen C, Lai C, Li N, Liu G, Wu D, Gao H, Hong L, Tan P, Chen S, Deng Z, Wu G, Wang L. mBio 11 e00488-20 (2020)
  8. S-Adenosylmethionine-responsive cystathionine β-synthase modulates sulfur metabolism and redox balance in Mycobacterium tuberculosis. Bandyopadhyay P, Pramanick I, Biswas R, Ps S, Sreedharan S, Singh S, Rajmani RS, Laxman S, Dutta S, Singh A. Sci Adv 8 eabo0097 (2022)
  9. Compounds with Potential Activity against Mycobacterium tuberculosis. Sao Emani C, Williams MJ, Wiid IJ, Baker B, Carolis C. Antimicrob Agents Chemother 62 e02236-17 (2018)
  10. Mycobacterium tuberculosis requires SufT for Fe-S cluster maturation, metabolism, and survival in vivo. Tripathi A, Anand K, Das M, O'Niel RA, P S S, Thakur C, R L RR, Rajmani RS, Chandra N, Laxman S, Singh A. PLoS Pathog 18 e1010475 (2022)
  11. The Effects of Serum hs-CRP on the Incidence of Lung Cancer in Male Patients with Pulmonary Tuberculosis. Jiang Y, Ni K, Fang M, Li J. Iran J Public Health 48 1265-1269 (2019)
  12. Expression, purification and function of cysteine desulfurase from Sulfobacillus acidophilus TPY isolated from deep-sea hydrothermal vent. Wang Y, Liu Q, Zhou H, Chen X. 3 Biotech 7 360 (2017)
  13. Roles of conserved active site residues in the IscS cysteine desulfurase reaction. Pang Y, Wang J, Gao X, Jiang M, Zhu L, Liang F, Liang M, Wu X, Xu X, Ren X, Xie T, Wang W, Sun Q, Xiong X, Lyu J, Li J, Tan G. Front Microbiol 14 1084205 (2023)
  14. Structural and Biochemical Characterization of Mycobacterium tuberculosis Zinc SufU-SufS Complex. Elchennawi I, Carpentier P, Caux C, Ponge M, Ollagnier de Choudens S. Biomolecules 13 732 (2023)


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