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Articles

Exploring the molecular insights of intrinsically disordered mitochondrial intermembrane protein in its unbound and substrate-bound state

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Pages 1239-1247 | Received 09 Dec 2019, Accepted 05 Aug 2020, Published online: 07 Sep 2020

References

  • Kaiser CM, Liu K. Folding up and moving on-nascent protein folding on the ribosome. J Mol Biol. 2018;430:4580–4591.
  • Redfern OC, Dessailly B, Orengo CA. Exploring the structure and function paradigm. Curr Opin Struct Biol. 2008;18:394–402.
  • Wright PE, Dyson HJ. Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm. J Mol Biol. 1999;293:321–331.
  • Dunker AK, Brown CJ, Lawson DJ, et al. Intrinsic disorder and protein function. Biochemistry. 2002;41:6573–6582.
  • Wright PE, Dyson HJ. Intrinsically disordered proteins in cellular signalling and regulation. Nature Reviews Molecular Cell Biology. 2015;16:18–29.
  • Van der Lee R, Buljan M, Lang B, et al. Classification of intrinsically disordered regions and proteins. Chem Rev. 2014;114:6589–6631.
  • Dunker AK, Obradovic Z. The protein trinity–linking function and disorder. Nat Biotechnol. 2001;19:805–806.
  • Babu MM, van der Lee R, de Groot NS, et al. Intrinsically disordered proteins: regulation and disease. Curr Opin Struct Biol. 2011;21:432–440.
  • Dyson HJ, Wright PE. Coupling of folding and binding for unstructured proteins. Curr Opin Struct Biol. 2002;12:54–60.
  • Kjaergaard M. Can proteins be intrinsically disordered inside a membrane? Intrinsically Disord Proteins. 2015;3:1–7.
  • Minezaki Y, Homma K, Nishikawa K. Intrinsically disordered regions of human plasma membrane proteins preferentially occur in the cytoplasmic segment. J Mol Biol. 2007;368:902–913.
  • Xue B, Liwei L, Meroueh SO, et al. Analysis of structured and intrinsically disordered regions of transmembrane proteins. Mol Biosyst. 2009;5:1688–1702.
  • Almén MS, Nordström KJ, Fredriksson R, et al. Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin. BMC Biol. 2009;7:1–14.
  • Hedin LE, Illergard K, Elofsson A. An Introduction to membrane proteins. J Proteome Res. 2011;10:3324–3331.
  • Hansen JC, Lu X, Ross ED, et al. Intrinsic protein disorder, amino acid composition, and histone terminal domains. J Biol Chem. 2006;281:1853–1856.
  • Hegedus T, Serohijos AW, Dokholyan NV, et al. Computational studies reveal phosphorylation-dependent changes in the unstructured R domain of CFTR. J Mol Biol. 2008;378:1052–1063.
  • Terziyska N, Lutz T, Kozany C, et al. Mia40, a novel factor for protein import into the intermembrane space of mitochondria is able to bind metal ions. FEBS Lett. 2005;579:179–184.
  • Banci L, Bertini I, Cefaro C, et al. Mia40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria. Nature Struct Mol Biol. 2009;16:198–206.
  • Banci L, Bertini I, Cefaro C, et al. Molecular chaperone function of Mia40 triggers consecutive induced folding steps of the substrate in mitochondrial protein import. PNAS. 2010;107:20190–20195.
  • Chacińska A, Pfannschmidt S, Wiedemann N, et al. Essential role of Mia40 in import and assembly of mitochondrial intermembrane space proteins. EMBO Jl. 2004;23:3735–3746.
  • Beers J, Glerum DM, Tzagoloff A. Purification, characterization, and localization of yeast Cox17, a mitochondrial copper shuttle. J Biol Chem. 1997;272:33191–33196.
  • Cobine PA, Pierrel F, Winge DR. Copper trafficking to the mitochondrion and assembly of copper metalloenzymes. Biochimica et Biophysica Acta (BBA). Mol Cell Res. 2006;1763:759–772.
  • Fraga H, Bech-Serra JJ, Canals F, et al. The mitochondrial intermembrane space oxidoreductase Mia40 funnels the oxidative folding pathway of cytochrome c oxidase assembly protein Cox19. J Biol Chem. 2014;289:9852–9864.
  • Fraga H, Pujols J, Gil-Garcia M, et al. Disulfide driven folding for a conditionally disordered protein. Scientific Rep. 2017;7:1–16.
  • Peleh V, Cordat E, Herrmann JM. Mia40 is a trans-site receptor that drives protein import into the mitochondrial intermembrane space by hydrophobic substrate binding. eLife. 2016;5:e16177.
  • Piovesan D, Tabaro F, Mičetić I, et al. Disprot 7.0: A major update of the database of disordered proteins. Nucleic Acids Res. 2017;45:D219–D227.
  • Roy A, Kucukural A, Zhang Y. I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc. 2010;5:725–738.
  • Yang J, Zhang Y. Protein structure and function prediction using I-TASSER. Current Protocols in Bioinformatics. 2015;52:5.8.1–5.8.15.
  • Kozakov D, Hall DR, Xia B, et al. The ClusPro web server for protein-protein docking. Nat Protoc. 2017;12:255–278.
  • Jo S, Kim T, Im W. Automated builder and database of protein/membrane complexes for molecular dynamics simulations. PLoS One. 2007;2(9):e880.
  • Jo S, Kim T, Iyer VG, et al. CHARMM-GUI: a web-based graphical user interface for CHARMM. J Comput Chem. 2008;29:1859–1865.
  • Klauda JB, Venable RM, Freites JA, et al. Update of the CHARMM all-atom additive force field for lipids: validation on six lipid types. J Phys Chem. 2010;114:7830–7843.
  • Jorgensen WL, Chandrasekhar J, Madura JD, et al. Comparison of simple potential functions for simulating liquid water. J Phys Chem. 1983;79:926–935.
  • Phillips JC, Braun R, Wang W, et al. Scalable molecular dynamics with NAMD. J Comput Chem. 2005;26:1781–1802.
  • Jo S, Lim JB, Klauda JB, et al. CHARMM-GUI membrane builder for mixed bilayers and its application to yeast membranes. Biophysical Jl. 2009;97:50–58.

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