Characteristics of the Isu1 C-terminus in relation to [2Fe-2S] cluster assembly and ISCU Myopathy
Tóm tắt
Mitochondrial [2Fe-2S] cluster biosynthesis is driven by the coordinated activities of the Iron–Sulfur Cluster (ISC) pathway protein machinery. Within the ISC machinery, the protein that provides a structural scaffold on which [2Fe-2S] clusters are assembled is the ISCU protein in humans; this protein is referred to as the “Scaffold” protein. Truncation of the C-terminal portion of ISCU causes the fatal disease “ISCU Myopathy”, which exhibits phenotypes of reduced Fe-S cluster assembly in cells. In this report, the yeast ISCU ortholog “Isu1” has been characterized to gain a better understanding of the role of the scaffold protein in relation to [2Fe-2S] assembly and ISCU Myopathy. Here we explored the biophysical characteristics of the C-terminal region of Isu1, the segment of the protein that is truncated on the human ortholog during the disease ISCU Myopathy. We characterized the role of this region in relation to iron binding, protein stability, assembly of the ISC multiprotein complex required to accomplish Fe-S cluster assembly, and finally on overall cell viability. We determined the Isu1 C-terminus is essential for the completion of the Fe-S cluster assembly but serves a function independent of protein iron binding.
Tài liệu tham khảo
Lill R, Freibert SA (2020) Annu Rev Biochem 89:471–499
Theil EC, Eisenstein RS (2000) J Biol Chem 275:40659–40662
Campbell CJ, Pall AE, Naik AR, Thompson LN, Stemmler TL (2021) Int J Mol Sci 22:6006
Braymer JJ, Lill R (2017) J Biol Chem 292:12754–12763
Rouault TA, Maio N (2017) J Biol Chem 292:12744–12753
Campuzano V, Montermini L, Molto MD, Pianese L, Cossee M, Cavalcanti F, Monros E, Rodius F, Duclos F, Monticelli A, Zara F, Canizares J, Koutnikova H, Bidichandani SI, Gellera C, Brice A, Trouillas P, De Michele G, Filla A, De Frutos R, Palau F, Patel PI, Di Donato S, Mandel JL, Cocozza S, Koenig M, Pandolfo M (1996) Science 271:1423–1427
Filla A, De Michele G, Cavalcanti F, Pianese L, Monticelli A, Campanella G, Cocozza S (1996) Am J Hum Genetics 59:554–560
Durr A, Cossee M, Agid Y, Campuzano V, Mignard C, Penet C, Mandel JL, Brice A, Koenig M (1996) N Engl J Med 335:1169–1175
Babcock M, de Silva D, Oaks R, Davis-Kaplan S, Jiralerspong S, Montermini L, Pandolfo M, Kaplan J (1997) Science 276:1709–1712
Foury F, Cazzalini O (1997) FEBS Lett 411:373–377
Rotig A, de Lonlay P, Chretien D, Foury F, Koenig M, Sidi D, Munnich A, Rustin P (1997) Nat Genet 17:215–217
Wang T, Craig EA (2008) J Biol Chem 283:12674–12679
Gerber J, Muhlenhoff U, Lill R (2003) EMBO Rep 4:906–911
Schilke B, Voisine C, Beinert H, Craig E (1999) Proc Natl Adad Aci USA 96:10206–10211
Frazzon J, Dean DR (2003) Curr Opin Chem Biol 7:166–173
Muhlenhoff U, Gerber J, Richhardt N, Lill R (2003) Embo J 22:4815–4825
Bridwell-Rabb J, Fox NG, Tsai CL, Winn AM, Barondeau DP (2014) Biochemistry 53:4904–4913
Pastore A, Puccio H (2013) J Neurochem 125:43–52
Cory SA, Van Vranken JG, Brignole EJ, Patra S, Winge DR, Drennan CL, Rutter J, Barondeau DP (2017) Proc Natl Acad Sci USA 114:E5325–E5334
Mochel F, Knight MA, Tong W-H, Hernandez D, Ayyad K, Taivassalo T, Andersen PM, Singleton A, Rouault TA, Fischbeck KH, Haller RG (2008) Am J Hum Genet 82:652–660
Drugge U, Holmberg M, Holmgren G, Almay BG, Linderholm H (1995) J Med Genet 32:344–347
Cook JD, Bencze KZ, Jankovic AD, Crater AK, Busch CN, Bradley PB, Stemmler AJ, Spaller MR, Stemmler TL (2006) Biochemistry 45:7767–7777
Patra S, Barondeau DP (2019) PNAS 116:19421–19430
Cook JD, Kondapalli KC, Rawat S, Childs WC, Murugesan Y, Dancis A, Stemmler TL (2010) Biochemistry 49:8756–8765
Cai K, Frederick RO, Tonelli M, Markley JL (2018) J Inorg Biochem 183:107–116
Fox NG, Yu X, Feng X, Bailey HJ, Martelli A, Nabhan JF, Strain-Damerell C, Bulawa C, Yue WW, Han S (2019) Nat Commun 10:2210
Cai K, Frederick RO, Tonelli M, Markley JL (2018) Biochemistry 57:1491–1500
Tsai CL, Barondeau DP (2010) Biochemistry 49:9132–9139
Leidgens S, De Smet S, Foury F (2010) Hum Mol Genet 19:276–286
Correia AR, Pastore C, Adinolfi S, Pastore A, Gomes CM (2008) FEBS J 275:3680–3690
Lewis BE, Mason Z, Rodrigues AV, Nuth M, Dizin E, Cowan JA, Stemmler TL (2019) Metallomics 11:1820–1835
Boniecki MT, Freibert SA, Muhlenhoff U, Lill R, Cygler M (2017) Nat Commun 8:1287
Ramelot TA, Cort JR, Goldsmith-Fischman S, Kornhaber GJ, Xiao R, Shastry R, Acton TB, Honig B, Montelione GT, Kennedy MA (2004) J Mol Biol 344:567–583
Liu J, Oganesyan N, Shin DH, Jancarik J, Yokota H, Kim R, Kim SH (2005) Proteins 59:875–881
Manicki M, Majewska J, Ciesielski S, Schilke B, Blenska A, Kominek J, Marszalek J, Craig EA, Dutkiewicz R (2014) JBC 289:30268–30278
Yoon H, Knight SA, Pandey A, Pain J, Turkarslan S, Pain D, Dancis A (2015) PLoS Genet 11:e1005135
Yoon H, Knight SAB, Pandey A, Pain J, Zhang Y, Pain D, Dancis A (2015) Biochem J 459:71–81
Li DS, Ohshima K, Jiralerspong S, Bojanowski MW, Pandolfo M (1999) FEBS Lett 456:13–16
Pohl T, Walter J, Stolpe S, Soufo JHD, Grauman PL, Friedrich T (2007) BMC Biochem 8:13
Dzul SP, Rocha AG, Rawat S, Kandegedara A, Kusowski A, Pain J, Murari A, Pain D, Dancis A, Stemmler TL (2017) Metallomics 9:48–60
Sreerama N, Woody RW (2004) Methods Enzymol 383:318–351
Privalov PL, Potekhin SA (1986) Methods Enzymol 131:4–51
Freibert S-A, Boniecki MT, Stümpfig C, Schulz V, Krapoth N, Winge DR, Mühlenhoff U, Stehling O, Cygler M, Lill R (2021) Nat Commun 12:6902
Ciesielski SJ, Schilke B, Marszalek J, Craig EA (2016) Mol Biol Cell 27:1060–1068
Markley JL, Kim JH, Dai Z, Bothe JR, Cai K, Frederick RO, Tonelli M (2013) FEBS Lett 587:1172–1179
Kim JH, Tonelli M, Kim T, Markley JL (2012) Biochemistry 51:5557–5563
Kim JH, Fuzery AK, Tonelli M, Ta DT, Westler WM, Vickery LE, Markley JL (2009) Biochemistry 48:6062–6071
Koebke KJ, Batelu S, Kandegedara A, Smith SR, Stemmler TL (2020) J Inorg Biochem 203:110882
Rodrigues AV, Kandegedara A, Rotondo JA, Dancis A, Stemmler TL (2015) Biometals 28:567–576
Bencze KZ, Kondapalli KC, Stemmler TL (2007). In: Scott RA, Lukehart CM (eds) Applications of physical methods in inorganic and bioinorganic chemistry: handbook, encyclopedia of inorganic chemistry, 2nd edn. John Wiley & Sons, LTD, Chichester, pp 513–528
Lewis BE (2019) Wayne State University Dissertations 2302. https://digitalcommons.wayne.edu/oa_dissertations/2302
Rodrigues AV (2014) Wayne State University Dissertations 1164:1–148. https://digitalcommons.wayne.edu/oa_dissertations/1164
Shimomura Y, Wada K, Fukuyama K, Takahashi Y (2008) J Mol Biol 383:133–143
Dutkiewicz R, Schilke B, Cheng S, Knieszner H, Craig EA, Marszalek J (2004) J Biol Chem 279:29167–29174
Kuzmic P (1996) Anal Biochem 237:260–273
George GN, George SJ and Pickering IJ (2001) http://www-ssrl.slac.stanford.edu/~george/exafspak/exafs.htm, Menlo Park, CA
Rehr JJ, Ankudinov AL (2001) J Synchrotron Radiat 8:61–65