Blue native PAGE
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Schägger, H. & von Jagow, G. Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal. Biochem. 199, 223–231 (1991).
Schägger, H., Cramer, W.A. & von Jagow, G. Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis. Anal. Biochem. 217, 220–230 (1994).
Schägger, H. Blue native electrophoresis, in Membrane Protein Purification and Crystallization. A Practical Guide 2nd edn. (eds. Hunte, C., von Jagow, G. & Schägger, H.) 5.105–5.130 (Academic, San Diego, USA, 2003).
Kügler, M., Jänsch, L., Kruft, V., Schmitz, U.K. & Braun, H.P. Analysis of the chloroplast protein complexes by blue-native polyacrylamide gelelectrophoresis. Photosynth. Res. 53, 35–44 (1997).
Schägger, H. Blue native gels to isolate protein complexes from mitochondria. Methods Cell Biol. 65, 231–244 (2001).
Pfeiffer, K. et al. Cardiolipin stabilizes respiratory chain supercomplexes. J. Biol. Chem. 278, 52873–52880 (2003).
Ludwig, J. et al. Identification and characterization of a novel 9.2 kDa membrane sector associated protein of vacuolar proton-ATPase from chromaffin granules. J. Biol. Chem. 273, 10939–10947 (1998).
Schägger, H. Native electrophoresis for isolation of mitochondrial oxidative phosphorylation protein complexes. Methods Enzymol. 260, 190–202 (1995).
Vahsen, N. et al. AIF deficiency compromises oxidative phosphorylation. EMBO J. 23, 4679–4689 (2004).
Acin-Perez, R. et al. Respiratory complex III is required to maintain complex I in mammalian mitochondria. Mol. Cell 13, 805–815 (2004).
Schägger, H. et al. Significance of respirasomes for the assembly/stability of human respiratory chain complex I. J. Biol. Chem. 279, 36349–36353 (2004).
Camacho-Carvajal, M., Wollscheid, B., Aebersold, R., Steimle, V. & Schamel, W.A. Two-dimensional blue native/SDS gel electrophoresis of multi-protein complexes from whole cellular lysates. Mol. Cell. Proteomics 3, 176–182 (2004).
Schägger, H. et al. Electrophoretic separation of multiprotein complexes from blood platelets and cell lines: Technique for the analysis of diseases with defects in oxidative phosphorylation. Electrophoresis 17, 709–714 (1996).
Schägger, H. Quantification of oxidative phosphorylation enzymes after blue native electrophoresis and two-dimensional resolution: Normal complex I protein amounts in Parkinson´s disease conflict with reduced catalytic activities. Electrophoresis 16, 763–770 (1995).
Carrozzo, R. et al. Subcomplexes of human ATP synthase mark mitochondrial biosynthesis disorders. Ann. Neurol. 59, 265–275 (2006).
Dudkina, N.V., Heinemeyer, J., Keegstra, W., Boekema, E.J. & Braun, H.P. Structure of dimeric ATP synthase from mitochondria: An angular association of monomers induces the strong curvature of the inner membrane. FEBS Lett. 579, 5769–5772 (2005).
Dudkina, N.V., Eubel, H., Keegstra, W., Boekema, E.J. & Braun, H.P. Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III. Proc. Natl. Acad. Sci. USA 102, 3225–3229 (2005).
Minauro-Sanmiguel, F., Wilkens, S. & Garcia, J.J. Structure of dimeric mitochondrial ATP synthase: novel FO bridging features and the structural basis of mitochondrial cristae biogenesis. Proc. Natl. Acad. Sci. USA 102, 12356–12358 (2005).
Schamel, W.W. et al. Coexistence of multivalent and monovalent TCRs explains high sensitivity and wide range of response. J. Exp. Med. 202, 493–503 (2005).
Arnold, I., Pfeiffer, K., Neupert, W., Stuart, R.A. & Schägger, H. Yeast mitochondrial F1FO-ATP synthase exists as a dimer: identification of three dimer-specific subunits. EMBO J. 17, 7170–7178 (1998).
Schägger, H. & Pfeiffer, K. Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 19, 1777–1783 (2000).
Stroh, A. et al. Assembly of respiratory chain complexes I, III, and IV into NADH oxidase supercomplex stabilizes Complex I in Paracoccus denitrificans. J. Biol. Chem. 279, 5000–5007 (2004).
Eubel, H., Jänsch, L. & Braun, H.P. New insights into the respiratory chain of plant mitochondria: supercomplexes and a unique composition of complex II. Plant Physiol. 133, 274–286 (2003).
Eubel, H., Heinemeyer, J. & Braun, H.P. Identification and characterization of respirasomes in potato mitochondria. Plant Physiol. 134, 1450–1459 (2004).
Paumard, P. et al. The ATP synthase is involved in generating mitochondrial cristae morphology. EMBO J. 21, 221–230 (2002).
Poetsch, A., Neff, D., Seelert, H., Schägger, H. & Dencher, N.A. Dye removal, catalytic activity and 2D-crystallization of chloroplast H+-ATP synthase purified by blue native electrophoresis. Biochim. Biophys. Acta 1466, 339–349 (2000).
Zerbetto, E., Vergani, L. & Dabbeni-Sala, F. Quantification of muscle mitochondrial oxidative phosphorylation enzymes via histochemical staining of blue native polyacrylamide gels. Electrophoresis 18, 2059–2064 (1997).
Jung, C., Higgins, C.M.J. & Xu, Z. Measuring the quantity of mitochondrial electron transport chain complexes in tissues of central nervous system using Blue native polyacrylamide gel electrophoresis. Anal. Biochem. 286, 214–223 (2000).
Eubel, H., Heinemeyer, J., Sunderhaus, S. & Braun, H.P. Respiratory chain supercomplexes in plant mitochondria. Plant Physiol. Biochem. 42, 937–942 (2004).
Sunderhaus, S. et al. Carbonic anhydrase subunits form a matrix-exposed domain attached to the membrane arm of mitochondrial complex I in plants. J. Biol. Chem. 281, 6482–6488 (2006).
Griffon, N. et al. Molecular determinants of glycine receptor subunit assembly. EMBO J. 18, 4711–4721 (1999).
Dietmeyer, K. et al. Tom 5 functionally links mitochondrial preprotein receptors to the general import pore. Nature 388, 195–200 (1997).
Jänsch, L., Kruft, V., Schmitz, U.K. & Braun, H.P. Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants. J. Biol. Chem. 273, 17251–17257 (1998).
Rais, I., Karas, M. & Schägger, H. Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification. Proteomics 4, 2567–2571 (2004).
Fandino, A.S. et al. LC-nanospray-MS/MS analysis of hydrophobic proteins from membrane protein complexes isolated by blue-native electrophoresis. J. Mass Spectrom. 40, 1223–1231 (2005).
Perales, M. et al. Disruption of a nuclear gene encoding a mitochondrial gamma carbonic anhydrase reduces complex I and supercomplex I+III2 levels and alters mitochondrial physiology in Arabidopsis. J. Mol. Biol. 350, 263–277 (2005).
Wittig, I. & Schägger, H. Advantages and limitations of clear native polyacrylamide gel electrophoresis. Proteomics 5, 4338–4346 (2005).
Gavin, P.D., Devenish, R.J. & Prescott, M. FRET reveals changes in the F1-stator stalk interaction during activity of F1FO-ATP synthase. Biochim. Biophys. Acta 1607, 167–179 (2003).
Gavin, P.D., Prescott, M. & Devenish, R.J. Yeast F1FO-ATP synthase complex interactions in vivo can occur in the absence of the dimer specific subunit e. J. Bioenerg. Biomembr. 37, 55–66 (2005).
Schägger, H. & von Jagow, G. Tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1–100 kDalton. Anal. Biochem. 166, 368–379 (1987).
Schägger, H. SDS electrophoresis techniques, in Membrane Protein Purification and Crystallization. A Practical Guide 2nd edn. (eds. Hunte, C., von Jagow, G. & Schägger, H.) 4.85–4.103 (Academic, San Diego, USA, 2003).
Werhahn, W. & Braun, H.P. Biochemical dissection of the mitochondrial proteome from Arabidopsis thaliana by three-dimensional gel electrophoresis. Electrophoresis 23, 640–646 (2002).
Studier, F.W. Analysis of bacteriophage T7 early RNAs and proteins on slab gels. J. Mol. Biol. 79, 237–248 (1973).
Hunkapiller, M.W., Lujan, E., Ostrander, F. & Hood, L.E. Isolation of microgram quantities of proteins from polyacrylamide gels for amino acid sequence analysis. Methods Enzymol. 91, 227–236 (1983).
Hjerten, S. Chromatographic separation according to size of macromolecules and cell particles on columns of agarose suspensions. Arch. Biochem. Biophys. 99, 466–475 (1962).
Reif, S., Voos, W. & Rassow, J. Intramitochondrial dimerization of citrate synthase characterized by blue native electrophoresis. Anal. Biochem. 288, 97–99 (2001).
Meisinger, C., Pfanner, N. & Truscott, K.N. Isolation of yeast mitochondria. Methods Mol. Biol. 313, 33–39 (2006).
Heinemeyer, J., Eubel, H., Wehmhöner, D., Jänsch, L. & Braun, H.P. Proteomic approach to characterize the supramolecular organization of photosystems in higher plants. Phytochemistry 65, 1683–1692 (2004).
Klose, J. & Kobalz, U. Two-dimensional electrophoresis of proteins: an updated protocol and implications for a functional analysis of the genome. Electrophoresis 16, 1034–1059 (1995).
Görg, A. & Weiss, W., High-resolution two-dimensional electrophoresis of proteins using immobilized pH gradients. in Cell Biology. A Laboratory Handbook (ed. Celis, J.) 386–397 (Academic, New York, 1998).
Laemmli, U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680–685 (1970).
Schägger, H., Brandt, U., Gencic, S. & von Jagow, G. Ubiquinol-cytochrome c-reductase from human and bovine mitochondria. Methods Enzymol. 260, 82–96 (1995).
Moro, F., Sirrenberg, C., Schneider, H.C., Neupert, W. & Brunner, M. The TIM17.23 preprotein translocase of mitochondria: composition and function in protein transport into the matrix. EMBO J. 18, 3667–3675 (1999).