Voltage-dependent Channels Found in the Membrane Fraction of Corn Mitochondria

Overview

Journal Plant Physiol

Specialty Physiology

Date 1985 Dec 1

PMID 16664537

Citations 23

Authors

D P Smack

M Colombini

Affiliations

Soon will be listed here.

Abstract

Transmembrane channels have been found in the membrane fraction of corn (Zea mays W64AN) mitochondria that exhibit a remarkable resemblance to the voltage dependent anion-selective channels (VDAC) located in the outer membrane of animal (Rattus norvegicus), protist (Paramecium aurelia), and fungal (Neurospora crassa) mitochondria. The channels in corn were demonstrated to be essentially identical to VDAC channels in three characteristic properties: (a) single channel conductance magnitude, (b) weak anion selectivity, and (c) nature of voltage dependence. These findings led us to conclude that the channels present in corn mitochondria are VDAC channels. This discovery may have repercussions concerning the regulation and function of higher plant mitochondria, and the causation of higher plant excitability.

Citing Articles

Solute Transport through Mitochondrial Porins In Vitro and In Vivo.

Benz R Biomolecules. 2024; 14(3).

PMID: 38540723 PMC: 10967727. DOI: 10.3390/biom14030303.

A charged existence: A century of transmembrane ion transport in plants.

Blatt M Plant Physiol. 2024; 195(1):79-110.

PMID: 38163639 PMC: 11060664. DOI: 10.1093/plphys/kiad630.

Identification and Characterization of VDAC Family in Maize.

Rodriguez-Saavedra C, Garcia-Ortiz D, Burgos-Palacios A, Morgado-Martinez L, King-Diaz B, Guevara-Garcia A Plants (Basel). 2023; 12(13).

PMID: 37447103 PMC: 10346152. DOI: 10.3390/plants12132542.

Historical Perspective of Pore-Forming Activity Studies of Voltage-Dependent Anion Channel (Eukaryotic or Mitochondrial Porin) Since Its Discovery in the 70th of the Last Century.

Benz R Front Physiol. 2022; 12:734226.

PMID: 35547863 PMC: 9083909. DOI: 10.3389/fphys.2021.734226.

Voltage-Dependent Anion Selective Channel Isoforms in Yeast: Expression, Structure, and Functions.

Di Rosa M, Guarino F, Conti Nibali S, Magri A, De Pinto V Front Physiol. 2021; 12:675708.

PMID: 34093236 PMC: 8171188. DOI: 10.3389/fphys.2021.675708.

References

WERKHEISER W, Bartley W . The study of steady-state concentrations of internal solutes of mitochondria by rapid centrifugal transfer to a fixation medium. Biochem J. 1957; 66(1):79-91. PMC: 1199968. DOI: 10.1042/bj0660079. View

Montal M, Mueller P . Formation of bimolecular membranes from lipid monolayers and a study of their electrical properties. Proc Natl Acad Sci U S A. 1972; 69(12):3561-6. PMC: 389821. DOI: 10.1073/pnas.69.12.3561. View

Pfaff E, Klingenberg M, RITT E, VOGELL W . [Correlation of the unspecific permeable mitochondrial space with the "intermembrane space"]. Eur J Biochem. 1968; 5(2):222-32. DOI: 10.1111/j.1432-1033.1968.tb00361.x. View

Mannella C, Colombini M, Frank J . Structural and functional evidence for multiple channel complexes in the outer membrane of Neurospora crassa mitochondria. Proc Natl Acad Sci U S A. 1983; 80(8):2243-7. PMC: 393795. DOI: 10.1073/pnas.80.8.2243. View

Colombini M . Structure and mode of action of a voltage dependent anion-selective channel (VDAC) located in the outer mitochondrial membrane. Ann N Y Acad Sci. 1980; 341:552-63. DOI: 10.1111/j.1749-6632.1980.tb47198.x. View

Zalman L, Nikaido H, Kagawa Y . Mitochondrial outer membrane contains a protein producing nonspecific diffusion channels. J Biol Chem. 1980; 255(5):1771-4. View

Roos N, Benz R, Brdiczka D . Identification and characterization of the pore-forming protein in the outer membrane of rat liver mitochondria. Biochim Biophys Acta. 1982; 686(2):204-14. DOI: 10.1016/0005-2736(82)90114-6. View

Mannella C . Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from Neurospora crassa mitochondria. J Cell Biol. 1982; 94(3):680-7. PMC: 2112230. DOI: 10.1083/jcb.94.3.680. View

Kimber A, Sze H . Helminthosporium maydis T Toxin Decreased Calcium Transport into Mitochondria of Susceptible Corn. Plant Physiol. 1984; 74(4):804-9. PMC: 1066772. DOI: 10.1104/pp.74.4.804. View

10.

Benz R, Janko K, Boos W, Lauger P . Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coli. Biochim Biophys Acta. 1978; 511(3):305-19. DOI: 10.1016/0005-2736(78)90269-9. View

11.

Moran N, Ehrenstein G, Iwasa K, Bare C, Mischke C . Ion channels in plasmalemma of wheat protoplasts. Science. 1984; 226(4676):835-8. DOI: 10.1126/science.6093255. View

12.

Freitag H, Neupert W, Benz R . Purification and characterisation of a pore protein of the outer mitochondrial membrane from Neurospora crassa. Eur J Biochem. 1982; 123(3):629-36. DOI: 10.1111/j.1432-1033.1982.tb06578.x. View

13.

Doring C, Colombini M . Voltage dependence and ion selectivity of the mitochondrial channel, VDAC, are modified by succinic anhydride. J Membr Biol. 1985; 83(1-2):81-6. DOI: 10.1007/BF01868740. View

14.

OBRIEN R, Brierley G . Compartmentation of heart mitochondria. I. Permeability characteristics of isolated beef heart mitochondria. J Biol Chem. 1965; 240(11):4527-31. View

15.

Colombini M . A candidate for the permeability pathway of the outer mitochondrial membrane. Nature. 1979; 279(5714):643-5. DOI: 10.1038/279643a0. View

16.

Wojtczak L, ZALUSKA H . On the impermeability of the outer mitochondrial membrane to cytochrome c. I. Studies on whole mitochondria. Biochim Biophys Acta. 1969; 193(1):64-72. DOI: 10.1016/0005-2736(69)90059-5. View

17.

Colombini M . Purification of VDAC (voltage-dependent anion-selective channel) from rat liver mitochondria. J Membr Biol. 1983; 74(2):115-21. DOI: 10.1007/BF01870500. View

18.

Schein S, Colombini M, Finkelstein A . Reconstitution in planar lipid bilayers of a voltage-dependent anion-selective channel obtained from paramecium mitochondria. J Membr Biol. 1976; 30(2):99-120. DOI: 10.1007/BF01869662. View

19.

Linden M, Andersson G, Gellerfors P, Nelson B . Subcellular distribution of rat liver porin. Biochim Biophys Acta. 1984; 770(1):93-6. DOI: 10.1016/0005-2736(84)90077-4. View