Abstract
Several limitations in transport properties of the outer mitochondrial membrane were found in intact mitochondria of porin-deficient mutants of S. cerevisiae, which grows as efficient as the isogenic wild strain. Restrictions concerned the effectiveness of ADP and CATR in triggering and terminating the phosphorylating state and of the external NADH in supporting the electron flow, with all three types of molecules apparently competing for the entry. These restrictions disappeared in mitoplasts obtained from mutant mitochondria. The existence of another pore is postulated. The novel pore seems to be controlled by cations which might act either directly on the pore or indirectly by screening the negative charge of the transported species. The novel pore is similarly sensitive to the synthetic polyanion as is VDAC; in the absence of VDAC the outer mitochondrial membrane is easily damaged by this inhibitor.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Benz R. (1985) Porin from bacterial and mitochondrial outer membranes. CRC Crit Rev in Biochem. 19, 145–190.
Benz R., Brdiczka D, (1992) The Cation-Selective Substrate of the Mitochondrial Outer Membrane Pore: Single-Channel Conductance and Influence on Inter-membrane and Peripheral Kinases. J. Bioenerg. Biomembr. 24, 33–39.
Benz R., Kottke M., Brdiczka D. (1990) The cationically selective state of the mitochondrial outer membrane pore: a study with intact mitochondria and reconstituted mitochondrial porin. Biochim. Biopnys. Acta 1022, 311–318.
Benz R., Schmid A., Dihanich M. (1989) Pores from mitochondrial outer membrane of yeast and a porin-deficient yeast mutant: A comparison. J. Bioenerg. Biomembr. 21, 439–450.
Benz R., Wojtczak L., Bosch W., Brdiczka D. (1988) Inhibition of adenine nucleotide transport through the mitochondrial porin by a synthetic polyanion. FEBS Lett. 231, 75–80.
Colombini M. (1979) A candidate for the permeability pathway of the outer mitochondrial membrane. Nature 279, 643–645.
Colombini M., Yeung C.L., Tung J., Konig T. (1987) The mitochondrial outer membrane channel, VDAC, is regulated by a synthetic polyanion. Biochim. BiophysActa 905, 279–286.
Daum G., Bohni P.C., Schatz G. (1982) Import of proteins into mitochondria. Cytochrome b2 and cytochrome c peroxidase are located in the intermem-brane space or yeast mitochondria. J. Biol. Chem. 257, 13028–13033.
De Pinto V., Zara V., Benz R., Gnoni G.V., Palmieri F. (1991) Characterization of pore-forming activity in liver mitochondria from Anguilla anguilla. Two porin in mitochondria? Biochim.Biophys.Acta 1061, 279–286.
Dihanich M., Schmid A., Oppeliger W., Benz R. (1989) Identification of a new pore in the mitochondrial outer membrane of a porin-deficent yeast mutant. Eur. J. Biochem. 181, 703–708.
Dihanich M., Suda K., Schatz G. (1987) A yeast mutant lacking mitochondrial porin is respiratory-deficient, but can recover respiration with simultaneous accumulation of an 86 kD extramitochondrial protein. EMBO J. 6, 723–728.
Douce R., Bourguignon J., Brouquisse R., Neuberger M. (1984) Isolation of plant mitochondria. General principles and criteria of integrity. Methods Enzymol. 148, 403–415.
Fevre F., Chich J-F., Lauquin G.J-M., Henry J-P., Thieffry M. (1990) Comparision of mitochondrial cationic channels in wild-type and porin-deficient mutant yeast. FEBS Lett. 262, 201–204.
Guo X.Y. (1988) Isolement et caracterisation du gene de la porine mitochondriale de S. cerevisiae. Etude de l’expression du gene et construction de mutants deficients en porine. D.Sc. thesis, University of Aix — Marseille II.
Guo X.J., Lauquin G.J-M. (1986) Mitochondrial porin-deficient mutant of S. cerevisiae: in vitro construction and preliminary properties. EBEC Reports 4, 292
Holden M.J., Colombini M. (1988) The mitochondrial outer membrane channel, VDAC, is modulated by a soluble protein. FEBS Lett. 241, 105–109.
Kamo N., Maratsugu M., Hongoh R., Kobatake Y. (1979) Membrane potential of mitochondria measured with an electron sensitive to tetraphenyl phosphonium and relationship between proton electrochemical potential and phosphorylation potential in steady state. J.Membr.Biol. 49, 105–121.
Liu M., Colombini M. (1991) Voltage gating of the mitochondrial outer membrane channel VDAC is regulated by a very conserved protein. AmJ.Physiol. 260, C371–C374.
Liu M.Y., Colombini M. (1992) Regulation of mitochondrial respiration by controlling the permeability of the outer membrane through the mitochondrial channel, VDAC, Biochim. Biophys.Acta 1098, 255–260.
Ludwig O., Benz R., Schultz J.E. (1989) Porin of Paramecium mitochondria isolation characterization and ion selectivity of the closed state. Biochim.Biophys. Acta 978, 319–327.
Mannella C. (1992) The “ins” and “outs” of mitochondrial membrane channels. TIBS 17, 315–320.
Michejda J., Guo X.J., Lauquin G.J-M. (1988) Energy coupling in cells and mitochondria of porin yeast mutants. EBEC Reports 5, 132
Michejda J., Guo X.J., Lauquin G.J-M. (1990) The respiration of cells and mitochondria of porin deficient yeast mutants is coupled. Biochem. Biophys. Res. Commun. 171, 354–361.
Nałęcz M., Nałęcz K., Azzi A (1991) Purification and functional characterization of the pyruvate (monocarboxylate) carrier from bakers yeast mitochondria (Saccharomyces cerevisiae). Biochim.Biophys.Acta 1079, 87–95.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1994 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Michejda, J., Kmita, H., Stobienia, O., Budzińska, M., Lauquin, G.JM. (1994). Restrictions of Metabolite Permeation Through the Outer Mitochondrial Membrane of Porin-Deficient Yeast Mutant. In: Forte, M., Colombini, M. (eds) Molecular Biology of Mitochondrial Transport Systems. NATO ASI Series, vol 83. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78936-6_24
Download citation
DOI: https://doi.org/10.1007/978-3-642-78936-6_24
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-78938-0
Online ISBN: 978-3-642-78936-6
eBook Packages: Springer Book Archive