Visualizing active membrane protein complexes by electron cryotomography
10.1038/ncomms5129
Crossref journal-article
Springer Science and Business Media LLC
Nature Communications (297)
Bibliography

Gold, V. A. M., Ieva, R., Walter, A., Pfanner, N., van der Laan, M., & Kühlbrandt, W. (2014). Visualizing active membrane protein complexes by electron cryotomography. Nature Communications, 5(1).

Authors 6
  1. Vicki A.M. Gold (first)
  2. Raffaele Ieva (additional)
  3. Andreas Walter (additional)
  4. Nikolaus Pfanner (additional)
  5. Martin van der Laan (additional)
  6. Werner Kühlbrandt (additional)
References 39 Referenced 64
  1. Wang, Q., Mercogliano, C. P. & Löwe, J. A ferritin-based label for cellular electron cryotomography. Structure 19, 147–154 (2011). (10.1016/j.str.2010.12.002) / Structure by Q Wang (2011)
  2. Mercogliano, C. P. & DeRosier, D. J. Concatenated metallothionein as a clonable gold label for electron microscopy. J. Struct. Biol. 160, 70–82 (2007). (10.1016/j.jsb.2007.06.010) / J. Struct. Biol. by CP Mercogliano (2007)
  3. Harrison, P. M. & Arosio, P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1275, 161–203 (1996). (10.1016/0005-2728(96)00022-9) / Biochim. Biophys. Acta by PM Harrison (1996)
  4. Mercogliano, C. P. & DeRosier, D. J. Gold nanocluster formation using metallothionein: mass spectrometry and electron microscopy. J. Mol. Biol. 355, 211–223 (2006). (10.1016/j.jmb.2005.10.026) / J. Mol. Biol. by CP Mercogliano (2006)
  5. Risco, C. et al. Specific, sensitive, high-resolution detection of protein molecules in eukaryotic cells using metal-tagging transmission electron microscopy. Structure 20, 759–766 (2012). (10.1016/j.str.2012.04.001) / Structure by C Risco (2012)
  6. Diestra, E., Fontana, J., Guichard, P., Marco, S. & Risco, C. Visualization of proteins in intact cells with a clonable tag for electron microscopy. J. Struct. Biol. 165, 157–168 (2009). (10.1016/j.jsb.2008.11.009) / J. Struct. Biol. by E Diestra (2009)
  7. Müller-Reichert, T. & Verkade, P. Correlative light and electron microscopy. Methods Cell Biol. 111, (2012).
  8. Hoffmann, C. et al. Fluorescent labeling of tetracysteine-tagged proteins in intact cells. Nat. Protoc. 5, 1666–1677 (2010). (10.1038/nprot.2010.129) / Nat. Protoc. by C Hoffmann (2010)
  9. Gaietta, G. M. et al. Golgi twins in late mitosis revealed by genetically encoded tags for live cell imaging and correlated electron microscopy. Proc. Natl Acad. Sci. USA 103, 17777–17782 (2006). (10.1073/pnas.0608509103) / Proc. Natl Acad. Sci. USA by GM Gaietta (2006)
  10. Deerinck, J. The application of fluorescent quantum dots to confocal, multiphoton, and electron microscopic imaging. Toxicol. Pathol. 36, 112–116 (2008). (10.1177/0192623307310950) / Toxicol. Pathol. by J Deerinck (2008)
  11. Nisman, R., Dellaire, G., Ren, Y., Li, R. & Bazett-Jones, D. P. Application of quantum dots as probes for correlative fluorescence, conventional, and energy-filtered transmission electron microscopy. J. Histochem. Cytochem. 52, 13–18 (2004). (10.1177/002215540405200102) / J. Histochem. Cytochem. by R Nisman (2004)
  12. Giepmans, B. N., Deerinck, T. J., Smarr, B. L., Jones, Y. Z. & Ellisman, M. H. Correlated light and electron microscopic imaging of multiple endogenous proteins using Quantum dots. Nat. Methods 2, 743–749 (2005). (10.1038/nmeth791) / Nat. Methods by BN Giepmans (2005)
  13. Mokranjac, D. & Neupert, W. The many faces of the mitochondrial TIM23 complex. Biochim. Biophys. Acta 1797, 1045–1054 (2010). (10.1016/j.bbabio.2010.01.026) / Biochim. Biophys. Acta by D Mokranjac (2010)
  14. Schmidt, O., Pfanner, N. & Meisinger, C. Mitochondrial protein import: from proteomics to functional mechanisms. Nat. Rev. Mol. Cell Biol. 11, 655–667 (2010). (10.1038/nrm2959) / Nat. Rev. Mol. Cell Biol. by O Schmidt (2010)
  15. Endo, T. & Yamano, K. Multiple pathways for mitochondrial protein traffic. Biol. Chem. 390, 723–730 (2009). (10.1515/BC.2009.087) / Biol. Chem. by T Endo (2009)
  16. Rassow, J. et al. Translocation arrest by reversible folding of a precursor protein imported into mitochondria - a means to quantitate translocation contact sites. J. Cell Biol. 109, 1421–1428 (1989). (10.1083/jcb.109.4.1421) / J. Cell Biol. by J Rassow (1989)
  17. Reichert, A. S. & Neupert, W. Contact sites between the outer and inner membrane of mitochondria—role in protein transport. Biochim. Biophys. Acta 1592, 41–49 (2002). (10.1016/S0167-4889(02)00263-X) / Biochim. Biophys. Acta by AS Reichert (2002)
  18. Dekker, P. J. et al. The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44. EMBO J. 16, 5408–5419 (1997). (10.1093/emboj/16.17.5408) / EMBO J. by PJ Dekker (1997)
  19. Mannella, C. A. Structure and dynamics of the mitochondrial inner membrane cristae. Biochim. Biophys. Acta 1763, 542–548 (2006). (10.1016/j.bbamcr.2006.04.006) / Biochim. Biophys. Acta by CA Mannella (2006)
  20. Zick, M., Rabl, R. & Reichert, A. S. Cristae formation-linking ultrastructure and function of mitochondria. Biochim. Biophys. Acta 1793, 5–19 (2009). (10.1016/j.bbamcr.2008.06.013) / Biochim. Biophys. Acta by M Zick (2009)
  21. Frank, J. Electron Tomography: Methods for Three-Dimensional Visualization of Structures in the Cell Springer Publishing (2008).
  22. Meeusen, S., McCaffery, J. M. & Nunnari, J. Mitochondrial fusion intermediates revealed in vitro. Science 305, 1747–1752 (2004). (10.1126/science.1100612) / Science by S Meeusen (2004)
  23. Wurm, C. A. et al. Nanoscale distribution of mitochondrial import receptor Tom20 is adjusted to cellular conditions and exhibits an inner-cellular gradient. Proc. Natl Acad. Sci. 108, 13546–13551 (2011). (10.1073/pnas.1107553108) / Proc. Natl Acad. Sci. by CA Wurm (2011)
  24. van der Laan, M., Bohnert, M., Wiedemann, N. & Pfanner, N. Role of MINOS in mitochondrial membrane architecture and biogenesis. Trends Cell Biol. 22, 185–192 (2012). (10.1016/j.tcb.2012.01.004) / Trends Cell Biol. by M van der Laan (2012)
  25. Vogel, F., Bornhövd, C., Neupert, W. & Reichert, A. S. Dynamic subcompartmentalization of the mitochondrial inner membrane. J. Cell Biol. 175, 237–247 (2006). (10.1083/jcb.200605138) / J. Cell Biol. by F Vogel (2006)
  26. Chacinska, A. et al. Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17. Cell 120, 817–829 (2005). (10.1016/j.cell.2005.01.011) / Cell by A Chacinska (2005)
  27. Tamura, Y. et al. Tim23-Tim50 pair coordinates functions of translocators and motor proteins in mitochondrial protein import. J. Cell Biol. 184, 129–141 (2009). (10.1083/jcb.200808068) / J. Cell Biol. by Y Tamura (2009)
  28. Wu, Y. & Sha, B. Crystal structure of yeast mitochondrial outer membrane translocon member Tom70p. Nat. Struct. Mol. Biol. 13, 589–593 (2006). (10.1038/nsmb1106) / Nat. Struct. Mol. Biol. by Y Wu (2006)
  29. Beckett, D., Kovaleva, E. & Schatz, P. J. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Prot. Sci. 8, 921–929 (1999). (10.1110/ps.8.4.921) / Prot. Sci. by D Beckett (1999)
  30. Lau, P. W., Potter, C. S., Carragher, B. & MacRae, I. J. DOLORS: versatile strategy for internal labeling and domain localization in electron microscopy. Structure. 20, 1995–2002 (2012). (10.1016/j.str.2012.10.019) / Structure. by PW Lau (2012)
  31. Dubavik, A. et al. Penetration of amphiphilic quantum dots through model and cellular plasma membranes. ACS Nano 6, 2150–2156 (2012). (10.1021/nn204930y) / ACS Nano by A Dubavik (2012)
  32. Koll, H. et al. Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 68, 1163–1175 (1992). (10.1016/0092-8674(92)90086-R) / Cell by H Koll (1992)
  33. Sikorski, R., S., & Hieter, P. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19–27 (1989). (10.1093/genetics/122.1.19) / Genetics by R Sikorski (1989)
  34. Meisinger, C., Pfanner, N. & Truscott, K. N. Isolation of yeast mitochondria. Methods Mol. Biol. 313, 33–39 (2006). / Methods Mol. Biol. by C Meisinger (2006)
  35. Gebert, M. et al. Mgr2 promotes coupling of the mitochondrial presequence translocase to partner complexes. J. Cell Biol. 197, 595–604 (2012). (10.1083/jcb.201110047) / J. Cell Biol. by M Gebert (2012)
  36. Kremer, J. R., Mastronade, D. N. & McIntosh, J. R. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116, 71–76 (1996). (10.1006/jsbi.1996.0013) / J. Struct. Biol. by JR Kremer (1996)
  37. Frangakis, A. S. & Hegerl, R. Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion. J. Struct. Biol. 135, 239–250 (2001). (10.1006/jsbi.2001.4406) / J. Struct. Biol. by AS Frangakis (2001)
  38. Thomsen, K. Surface Area of an Ellipsoid www.numericana.com (2004).
  39. Nicastro, D. et al. The molecular architecture of axonemes revealed by cryoelectron tomography. Science 313, 944–948 (2006). (10.1126/science.1128618) / Science by D Nicastro (2006)
Dates
Type When
Created 11 years, 2 months ago (June 19, 2014, 6:57 a.m.)
Deposited 2 years, 7 months ago (Jan. 5, 2023, 10:36 p.m.)
Indexed 2 months, 4 weeks ago (May 29, 2025, 1:24 p.m.)
Issued 11 years, 2 months ago (June 19, 2014)
Published 11 years, 2 months ago (June 19, 2014)
Published Online 11 years, 2 months ago (June 19, 2014)
Funders 0

None

@article{Gold_2014, title={Visualizing active membrane protein complexes by electron cryotomography}, volume={5}, ISSN={2041-1723}, url={http://dx.doi.org/10.1038/ncomms5129}, DOI={10.1038/ncomms5129}, number={1}, journal={Nature Communications}, publisher={Springer Science and Business Media LLC}, author={Gold, Vicki A.M. and Ieva, Raffaele and Walter, Andreas and Pfanner, Nikolaus and van der Laan, Martin and Kühlbrandt, Werner}, year={2014}, month=jun }