Iron loading site on the Fe-S cluster assembly scaffold protein is distinct from the active site

BioMetals

Volumn 28, Issue 3, 2015, Pages 567-576

  Rodrigues, Andria V ^a   Kandegedara, Ashoka ^a   Rotondo, John A ^a   Dancis, Andrew ^b   Stemmler, Timothy L ^a  

^a WAYNE STATE UNIVERSITY   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Fe S cluster biosynthesis; Iron; Iron binding; ISU scaffold protein

Indexed keywords

IRON; IRON SULFUR PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

ENZYME ACTIVE SITE; METABOLISM; SACCHAROMYCES CEREVISIAE;

CATALYTIC DOMAIN; IRON; IRON-SULFUR PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 84939992480     PISSN: 09660844     EISSN: 15728773     Source Type: Journal    
DOI: 10.1007/s10534-015-9846-8     Document Type: Article

References (23)

1. Bencze KZ, Kondapalli KC, Cook JD, McMahon S, Millan-Pacheco C, Pastor N, Stemmler TL (2006) The structure and function of frataxin. Crit Rev Biochem Mol Biol 41(5):269-291. doi: 10.1080/10409230600846058
2. Bencze KZ, Kondapalli KC, Stemmler TL (2007) X-ray absorption spectroscopy. In: Scott RA, Lukehart CM (eds) Applications of physical methods in inorganic and bioinorganic chemistry: handbook, encyclopedia of inorganic chemistry, 2nd edn. Wiley, Chichester, pp 513-528
3. Bertini I, Cowan JA, Del Bianco C, Luchinat C, Mansy SS (2003) Thermotoga maritima IscU. Structural characterization and dynamics of a new class of metallochaperone. J Mol Biol 331(4):907-924. doi: 10.1016/S0022-2836(03)00768-X
4. Bridwell-Rabb J, Fox NG, Tsai CL, Winn AM, Barondeau DP (2014) Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry. Biochemistry 53(30):4904-4913. doi: 10.1021/bi500532e
5. Cook JD, Bencze KZ, Jankovic AD, Crater AK, Busch CN, Bradley PB, Stemmler AJ, Spaller MR, Stemmler TL (2006) Monomeric yeast frataxin is an iron-binding protein. Biochemistry 45(25):7767-7777. doi: 10.1021/bi060424r
6. Cook JD, Kondapalli KC, Rawat S, Childs WC, Murugesan Y, Dancis A, Stemmler TL (2010) Molecular details of the yeast frataxin-Isu1 interaction during mitochondrial Fe-S cluster assembly. Biochemistry 49(40):8756-8765. doi: 10.1021/bi1008613
7. Craig EA, Voisine C, Schilke B (1999) Mitochondrial iron metabolism in the yeast Saccharomyces cerevisiae. Biol Chem 380(10):1167-1173. doi: 10.1515/BC.1999.148
8. 2+ center of possible functional significance. J Am Chem Soc 122:6805-6806. doi: 10.1021/ja000800.
9. Garland SA, Hoff K, Vickery LE, Culotta VC (1999) Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assembly. J Mol Biol 294(4):897-907. doi: 10.1006/jmbi.1999.3294
10. Grzesiak A, Helland R, Smalas AO, Krowarsch D, Dadlez M, Otlewski J (2000) Substitutions at the P(1) position in BPTI strongly affect the association energy with serine proteinases. J Mol Biol 301(1):205-217. doi: 10.1006/jmbi.2000.3935
11. Holmes-Hampton GP, Miao R, Garber Morales J, Guo Y, Munck E, Lindahl PA (2010) A nonheme high-spin ferrous pool in mitochondria isolated from fermenting Saccharomyces cerevisiae. Biochemistry 49(19):4227-4234. doi: 10.1021/bi1001823
12. Johnson DC, Dean DR, Smith AD, Johnson MK (2005) Structure, function, and formation of biological iron-sulfur clusters. Annu Rev Biochem 74:247-281. doi: 10.1146/annurev.biochem.74.082803.133518
13. Kim JH, Fuzery AK, Tonelli M, Ta DT, Westler WM, Vickery LE, Markley JL (2009) Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB. Biochemistry 48(26):6062-6071. doi: 10.1021/bi9002277
14. Kuzmic P (1996) Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal Biochem 237:260-273. doi: 10.1006/abio.1996.0238
15. Lill R (2009) Function and biogenesis of iron-sulphur proteins. Nature 460(7257):831-838. doi: 10.1038/nature08301
16. Lill R, Hoffmann B, Molik S, Pierik AJ, Rietzschel N, Stehling O, Uzarska MA, Webert H, Wilbrecht C, Muhlenhoff U (2012) The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism. Biochim Biophys Acta 1823(9):1491-1508. doi: 10.1016/j.bbamcr.2012.05.009
17. Raulfs EC, O'Carroll IP, Dos Santos PC, Unciuleac MC, Dean DR (2008) In vivo iron-sulfur cluster formation. Proc Natl Acad Sci USA 105(25):8591-8596. doi: 10.1073/pnas.0803173105
18. Rouault TA (2014) Mammalian iron-sulphur proteins: novel insights into biogenesis and function. Nat Rev Mol Cell Biol. doi: 10.1038/nrm3909
19. Shi R, Proteau A, Villarroya M, Moukadiri I, Zhang L, Trempe JF, Matte A, Armengod ME, Cygler M (2010) Structural basis for Fe-S cluster assembly and tRNA thiolation mediated by IscS protein-protein interactions. PLoS Biol 8(4):1-18. doi: 10.1371/journal.pbio.1000354
20. Simons TJ (1993) Measurement of Zn(II) ion concentration with fluorescence probe magfura-2. J Biochem Biophys Methods 27:25-37. doi: 10.1016/0165-022X(93)90065-V
21. Stehling O, Lill R (2013) The role of mitochondria in cellular iron-sulfur protein biogenesis: mechanisms, connected processes, and diseases. Cold Spring Harb Perspect Biol 5(8):1-17. doi: 10.1101/cshperspect.a011312
22. Stehling O, Wilbrecht C, Lill R (2014) Mitochondrial iron-sulfur protein biogenesis and human disease. Biochimie 100:61-77. doi: 10.1016/j.biochi.2014.01.010
23. Walkup GK, Imperiali B (1997) Fluorescent chemosensors for divalent zinc based on zinc finger domains. J Am Chem Soc 119:3443-3450. doi: 10.1021/ja9642121