PH-induced conformational change of IscU at low pH correlates with protonation/deprotonation of two conserved histidine residues

Biochemistry

Volumn 53, Issue 32, 2014, Pages 5290-5297

  Dai, Ziqi ^a   Kim, Jin Hae ^a,b   Tonelli, Marco ^a   Ali, Ibrahim K ^a   Markley, John L ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; ESCHERICHIA COLI; PROTEINS; PROTONS; SCAFFOLDS (BIOLOGY); SULFUR;

BIOSYNTHESIS PATHWAYS; CONFORMATIONAL CHANGE; CONFORMATIONAL STATE; HISTIDINE RESIDUES; IRON-SULFUR CLUSTERS; PEPTIDE BONDS; PROTON AFFINITY; SCAFFOLD PROTEIN;

AMINO ACIDS;

HISTIDINE; IRON; ISCU PROTEIN; MEMBRANE PROTEIN; PROTON; SULFUR; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CATION TRANSPORT; CONFORMATIONAL TRANSITION; DEPROTONATION; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PH; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTON TRANSPORT; TITRIMETRY;

AMINO ACID SEQUENCE; CONSERVED SEQUENCE; ESCHERICHIA COLI PROTEINS; HISTIDINE; HYDROGEN-ION CONCENTRATION; IRON-SULFUR PROTEINS; PROTEIN CONFORMATION;

EID: 84906244550     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500313t     Document Type: Article

References (27)

1. Lill, R. (2009) Function and biogenesis of iron-sulphur proteins Nature 460, 831-838
2. Ayala-Castro, C., Saini, A., and Outten, F. W. (2008) Fe-S cluster assembly pathways in bacteria Microbiol. Mol. Biol. Rev. 72, 110-125
3. Johnson, M. K. (1998) Iron-sulfur proteins: new roles for old clusters Curr. Opin. Chem. Biol. 2, 173-181
4. Kim, J. H., Tonelli, M., and Markley, J. L. (2012) Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase Proc. Natl. Acad. Sci. U.S.A. 109, 454-459
5. Rouault, T. A. and Tong, W. H. (2008) Iron-sulfur cluster biogenesis and human disease Trends Genet. 24, 398-407
6. Sheftel, A., Stehling, O., and Lill, R. (2010) Iron-sulfur proteins in health and disease Trends Endocrinol. Metab. 21, 302-314
7. Shi, Y., Ghosh, M. C., Tong, W. H., and Rouault, T. A. (2009) Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis Hum. Mol. Genet. 18, 3014-3025
8. Campuzano, V., Montermini, L., Molto, M. D., Pianese, L., Cossee, M., Cavalcanti, F., Monros, E., Rodius, F., Duclos, F., Monticelli, A., Zara, F., Canizares, J., Koutnikova, H., Bidichandani, S. I., Gellera, C., Brice, A., Trouillas, P., De Michele, G., Filla, A., De Frutos, R., Palau, F., Patel, P. I., Di Donato, S., Mandel, J. L., Cocozza, S., Koenig, M., and Pandolfo, M. (1996) Friedreichs ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion Science 271, 1423-1427
9. Ramelot, T. A., Cort, J. R., Goldsmith-Fischman, S., Kornhaber, G. J., Xiao, R., Shastry, R., Acton, T. B., Honig, B., Montelione, G. T., and Kennedy, M. A. (2004) Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site J. Mol. Biol. 344, 567-583
10. Shimomura, Y., Kamikubo, H., Nishi, Y., Masako, T., Kataoka, M., Kobayashi, Y., Fukuyama, K., and Takahashi, Y. (2007) Characterization and crystallization of an IscU-type scaffold protein with bound [2Fe-2S] cluster from the hyperthermophile Aquifex aeolicus J. Biochem. 142, 577-586
11. Wu, G., Mansy, S. S., Wu, S. P., Surerus, K. K., Foster, M. W., and Cowan, J. A. (2002) Characterization of an iron-sulfur cluster assembly protein (ISU1) from Schizosaccharomyces pombe Biochemistry 41, 5024-5032
12. Shimomura, Y., Wada, K., Fukuyama, K., and Takahashi, Y. (2008) The asymmetric trimeric architecture of [2Fe-2S] IscU: implications for its scaffolding during iron-sulfur cluster biosynthesis J. Mol. Biol. 383, 133-143
13. Unciuleac, M. C., Chandramouli, K., Naik, S., Mayer, S., Huynh, B. H., Johnson, M. K., and Dean, D. R. (2007) In vitro activation of apo-aconitase using a [4Fe-4S] cluster-loaded form of the IscU [Fe-S] cluster scaffolding protein Biochemistry 46, 6812-6821
14. Foster, M. W., Mansy, S. S., Hwang, J., Penner-Hahn, J. E., Surerus, K. K., and Cowan, J. A. (2000) A mutant human IscU protein contains a stable [2Fe-2S](2+) center of possible functional significance J. Am. Chem. Soc. 122, 6805-6806
15. Kim, J. H., Füzéry, A. K., Tonelli, M., Ta, D. T., Westler, W. M., Vickery, L. E., and Markley, J. L. (2009) Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB Biochemistry 48, 6062-6071
16. Kim, J. H., Tonelli, M., Kim, T., and Markley, J. L. (2012) Three-dimensional structure and determinants of stability of the iron-sulfur cluster scaffold protein IscU from Escherichia coli Biochemistry 51, 5557-5563
17. Kim, J. H., Tonelli, M., Frederick, R. O., Chow, D. C., and Markley, J. L. (2012) Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU) J. Biol. Chem. 287, 31406-31413
18. Kim, J. H., Bothe, J. R., Frederick, R. O., Holder, J. C., and Markley, J. L. (2014) Role of IscX in iron-sulfur cluster biogenesis in Escherichia coli J. Am. Chem. Soc. 136, 7933-7942
19. Markley, J. L., Kim, J. H., Dai, Z., Bothe, J. R., Cai, K., Frederick, R. O., and Tonelli, M. (2013) Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron-sulfur cluster biosynthesis and delivery FEBS Lett. 587, 1172-1179
20. Dai, Z., Tonelli, M., and Markley, J. L. (2012) Metamorphic protein IscU changes conformation by cis-trans isomerizations of two peptidyl-prolyl peptide bonds Biochemistry 51, 9595-9602
21. Hoff, K. G., Silberg, J. J., and Vickery, L. E. (2000) Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 97, 7790-7795
22. Füzéry, A. K., Tonelli, M., Ta, D. T., Cornilescu, G., Vickery, L. E., and Markley, J. L. (2008) Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU Biochemistry 47, 9394-9404
23. Bonomi, F., Iametti, S., Morleo, A., Ta, D., and Vickery, L. E. (2008) Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones Biochemistry 47, 12795-12801
24. Lee, W., Yu, W., Kim, S., Chang, I., Lee, W., and Markley, J. L. (2012) PACSY, a relational database management system for protein structure and chemical shift analysis J. Biomol. NMR 54, 169-179
25. Hilge, M., Siegal, G., Vuister, G., Guentert, P., Gloor, S., and Abrahams, J. (2003) ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase Nat. Struct. Biol. 10, 468-474
26. Shi, R., Proteau, A., Villarroya, M., Moukadiri, I., Zhang, L., Trempe, J. F., Matte, A., Armengod, M. E., and Cygler, M. (2010) Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions PLoS Biol. 8, 18
27. Kornhaber, G. J., Swapna, G. V. T., Ramelot, T. A., Cort, J. R., Aramini, J. M., Kennedy, M. A., and Montelione, G. T. (2011) Solution NMR Structure of Zn-Ligated Fe-S Cluster Assembly Scaffold Protein SufU from Bacillus subtilis. PDB entry 2azh, DOI: 10.2210/pdb2azh/pdb.