Abstract
The cell envelope of Gram-negative bacteria consists of three different layers, the outer membrane, the murein and the inner membrane (Beveridge, 1981). The inner membrane represents a real diffusion barrier and contains, similar to the mitochondrial inner membrane, the respiration chain and a large number of transport systems. The outer membrane of Gram-negative bacteria plays an important role in the physiology of these organisms. All nutrients or antibiotics either hydrophilic or hydrophobic have to cross this permeability barrier which means that it has special sieving properties. The active components of molecular sieving of the outer membrane are due to presence of a few major proteins called “porins” (Nakae, 1976). The porins are organized as trimers of three identical subunits and form transmembrane channels that have more general properties and sort according to the molecular weight of the solutes (Benz, 1985; Nikaido & Vaara, 1985). On the other hand, also specific porins have been identified in the outer membrane of Gram-negative bacteria which contain binding sites for substrates (Benz, 1988). The porin trimers form basically one channel in the outer membrane with three openings faced to the cell surface and one outlet into the periplasmic space (Engel et al., 1985; Lepault et al., 1988).
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References
Benz R (1985) Porins from bacterial and mitochondrial outer membranes. CRC Crit Rev Biochem 19:145–190
Benz R (1988) Structure and function of porins from Gram-negative bacteria. Ann Rev Microbiol 42:359–393
Benz R, Janko K, Boos W, Läuger P (1978) Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta 511:305–319
Benz R, Janko K, Läuger P (1979) Ionic selectivity of pores formed by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta 551:238–247
Benz R, Ludwig O, De Pinto V, Palmieri F (1985) Permeability properties of mitochondrial porins of different eukaryotic cells. In: Quagliariello E et al. (eds) Achievements and Perspectives of Mitochondrial Research, vol 1. Elsevier, Amsterdam, pp 317–327
Benz R, Schmid A, Hancock REW (1985) Ion selectivity of Gram-negative bacterial porins. J Bacteriol 162:722–727
Benz R, Schmid A, Vos-Scheperkeuter GH (1987) Mechanism of sugar transport through the sugar-specific LamB channel of Escherichia coli outer membrane. J Membrane Biol 100:12–29
Benz R, Wojtczak L, Bosch W, Brdiczka D (1988) Inhibition of adenine nucleotide transport through the mitochondrial porin by a synthetic polyanion. FEBS Lett 210:75–80
Bessman SP, Carpenter CL, (1985) The creatine-phosphate energy shuttle. Ann Rev Cytochem 54:831–865
Beveridge TJ (1981) Ultrastructure, chemistry and function of the bacterial wall. Int Rev Cytol 72:229–317
Brdiczka D, Knoll G, Riesinger I, Weiler U, Klug G, Benz R, Krause J (1986) Micro-compartmentation at the mitochondrial surface: its function in metabolic regulation. Myocardial and skeletal muscle bioenergetics. Brautbar N (ed) Plenum Press, New York, pp 55–69
Brdiczka D, Adams V, Kottke M, Benz R (1989) Topology of peripheral kinases: Its importance in transmission of mitochondrial energy. In: Azzi A, Nałęcz KA, Nałęcz MJ, Wojtczak L (eds) The Anion Carriers of the Mitochondrial Membranes. Springer-Verlag Heidelberg, pp 361-372
Brooks SPJ, Suelter CH (1987) Compartmented coupling of chicken heart creatine kinase to the nucleotide translocase requires the outer membrane. Arch Biochem Biophys 257:144–153
Colombini M (1979) A candidate for the permeability pathway of the outer mitochondrial membrane. Nature 279:643–645
Colombini M (1980) Pore size and properties of channels from mitochondria isolated from Neurospora crossa. J Membrane Biol 53:79–84
De Pinto V, Ludwig O, Krause J, Benz R, Palmieri F (1987a) Porin pores of mitochondrial outer membranes from high and low eukaryotic cells: biochemical and biophysical characterization. Biochim Biophys Acta 894:109–119
De Pinto V, Prezioso G, Palmieri F (1987b) A simple and rapid method for the purification of the mitochondrial porin from mammalian sources. Biochim Biophys Acta 905:499–502
De Pinto V (1989) Purification of mammalian porins In: Azzi A, Nałcz KA, Nałcz MJ, Wojtczak L (eds) The Anion Carriers of the Mitochondrial Membranes. Springer-Verlag Heidelberg, pp 237-248
Engel A, Massalski A, Schindler M, Dorset DL, Rosenbusch, JP (1985) Porin channels merge into single outlets in Escherichia coli outer membranes. Nature 317:643–645
Fiek C, Benz R, Roos N, Brdiczka D (1982) Evidence for identity between the hexoki-nase-binding protein and the mitochondrial porin in the outer membrane of rat liver mitochondria. Biochim Biophys Acta 688:429–440
Freitag H, Janes M, Neupert W (1982a) Biosynthesis of mitochondrial porin and insertion into the outer mitochondrial membrane of Neurospora crossa. Eur J Biochem 126:197–202
Freitag H, Neupert W, Benz R (1982b) Purification and characterization of a pore protein of the outer mitochondrial membrane from Neurospora crossa. Eur J Biochem 123:629–636
Gellerich FN, Schlame M, Bohnensack R, Kunz W (1987) Dynamic compartmentation of adenine nucleotides in the mitochondrial intermembrane space of rat-heart mitochondria. Biochim Biophys Acta 890:117–126
Hancock REW (1986) Model membrane studies of porin function. In: Inouye M (ed) Bacterial outer Membranes as Model Systems. Wiley and Sons, New York, pp 187–225
Hancock REW, Benz R (1986) Demonstration and chemical modification of a specific phosphate binding site in the phosphate-starvation-inducible outer membrane porin protein P of Pseudomonas aeruginosa. Biochim Biophys Acta 860:699–707
Hancock REW, Poole K, Benz R (1982) Outer membrane protein P of Pseudomonas aeniginosa: regulation by phosphate deficiency and formation of small anion-specific channels in lipid bilayer membranes. J Bacteriol 150:730–738
Kleene R, Pfanner N, Pfaller R, Link TA, Sebald W, Neupert W, Tropschug M (1987) Mitochondrial porin of Neurospora crossa: cDNA cloning, in vitro expression and import into mitochondria. EMBO J 9:2627–2633
Lepault J, Dargent B, Tichelaar W, Rosenbusch JP, Leonard K, Pattus F (1988) Three dimensional reconstitution of maltoporin from electron microscopy and image processing. EMBO J 7:261–268
Lindén M, Gellerfors P, Nelson BD (1982a) Purification of a protein having pore forming activity from the rat liver mitochondrial outer membrane. Biochem J 208:77–82
Lindén M, Gellerfors P, Nelson BD (1982b) Pore protein and hexokinase-binding protein from the outer membrane of rat liver mitochondria are identical. FEBS Lett 141:189–192
Luckey M, Nikaido H (1980) Specificity of diffusion channels produced by-phage receptor protein of Escherichia coli. Proc Natl Acad Sci (USA) 77:167–171
Ludwig O, Krause J, Hay R, Benz R (1988a) Purification and characterization of the pore forming protein of yeast mitochondrial outer membrane. Eur Biophys J 15:269–276
Ludwig O, Benz R, Schultz IE (1988b) Porin of Paramecium mitochondria: Isolation characterization and ion selectivity of the closed state. Eur J Biochem (submitted)
Maier C, Bremer E, Schmid A, Benz R (1987) Pore-forming activity of the Tsx protein from the outer membrane of Escherichia coli. Demonstration of a nucleoside-specific binding site. J Biol Chem 263:2493–2499
Mannella CA, Frank J (1984a) Negative staining characteristics of arrays of mitochondrial pore protein: Use of correspondence analysis to classify different staining patterns. Ultramicroscopy 13:93–102
Mannella CA, Frank J (1984b) Electron microscopic stains as probes of the surface charge of mitochondrial outer membrane channels. Biophys J 45:139–141
Mihara K, Sato R (1985) Molecular cloning and sequencing of cDNA of yeast porin, an outer mitochondrial membrane protein: a search for targeting signal in the primary structure. EMBO J 4:769–774
Nakae T (1976) Identification of the major outer membrane protein of Escherichia coli that produces transmembrane channels in reconstituted vesicle membranes. Biochem Biophys Res Commun 71:877–884
Nikaido H (1983) Proteins forming large channels from bacterial and mitochondrial outer membranes: Porins and phage lambda receptor protein. Methods Enzymol 97:85–100
Nikaido H, Rosenberg EY (1983) Porin channels in Escherichia coli: studies with liposomes reconstituted from purified proteins. J Bacteriol 153:241–252
Nikaido H, Rosenberg EY, Foulds J (1983) Porin channels in Escherichia coli: studies with β-lactams in intact cells. J Bacteriol 153:232–240
Nikaido H, Vaara M (1985) Molecular basis of bacterial outer membrane permeability. Microbiol Rev 49:1–32
Ohlendieck K, Riesinger I, Adams V, Krause J, Brdiczka D (1986) Enrichment and biochemical characterization of boundary membrane contact sites in rat-liver mitochondria. Biochim Biophys Acta 860:672–689
Roos AK, Benz R, Brdiczka D (1982) Identification and characterization of the poreforming protein in the outer membrane of rat liver mitochondria. Biochim Biophys Acta 686:204–214
Schein SJ, Colombini M, Finkelstein A (1976) Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from Paramecium mitochondria. J Membrane Biol 30:99–120
Schindler H, Rosenbusch JP (1978) Matrix protein from Escherichia coli outer membranes forms voltage-controlled channels in lipid bilayers. Proc Natl Acad Sci (USA) 75:3751–3755
Sen K, Hellman J, Nikaido H (1988) Porin channels in intact cell of Escherichia coli are not affected by Donnan potentials across the outer membrane. J Biol Chem 263:1182–1187
Szmelcman S, Hofnung M (1975) Maltose transport in Escherichia coli K-12: Involvement of the bacteriophage lambda receptor. J Bacteriol 124:112–118
Tommassen J, Lugtenberg B (1980) Outer membrane protein e of Escherichia coli K-12 is coregulated with alkaline phosphatase. J Bacteriol 143:151–157
Wojtczak L, Zaluska H (1969) On the impermeability of the outer mitochondrial membrane to cytochrome c: I. Studies on whole mitochondria. Biochim Biophys Acta 193:64–72
Zalman LS, Nikaido H, Kagawa Y (1980) Mitochondrial outer membrane contains a protein producing nonspecific diffusion channels. J Biol Chem 255:1771–1774
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Benz, R. (1989). Porins from Mitochondrial and Bacterial Outer Membranes: Structural and Functional Aspects. In: Azzi, A., Nałęz, K.A., Nałęcz, M.J., Wojtczak, L. (eds) Anion Carriers of Mitochondrial Membranes. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-74539-3_16
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DOI: https://doi.org/10.1007/978-3-642-74539-3_16
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