Journal of Bioenergetics and Biomembranes

, Volume 24, Issue 1, pp 55–61 | Cite as

Binding of a synthetic targeting peptide to a mitochondrial channel protein

  • Carmen A. Mannella
  • Xiao Wei Guo
  • James Dias
Research Paper


Membrane crystals of the mitochondrial outer membrane channel VDAC (porin) fromNeurospora crassa were incubated with a 20-amino-acid synthetic peptide corresponding to the N-terminal targeting region of subunit IV of cytochrome oxidase. The peptide caused disordering and contraction of the crystal lattice of the membrane arrays. Also, new stain-excluding features were observed on the peptide-treated arrays which most likely correspond to sites at which the peptide accumulates. The stain exclusion zones associated with binding of the targeting peptide (and with binding of apocytochromec in an earlier study) have been localized on a two-dimensional density map of frozen-hydrated, crystalline VDAC previously obtained by cryo-electron microscopy. The results indicate that both the peptide and cytochromec bind to protein “arms” which extend laterally between the channel lumens. The finding that imported polypeptides bind to a specific region of the VDAC protein implicates this channel in the process by which precursor proteins are recognized at and translocated across the mitochondrial outer membrane.

Key words

Mitochondrial channels mitochondrial targeting sequences electron microscopy computer image processing 


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Copyright information

© Plenum Publishing Corporation 1992

Authors and Affiliations

  • Carmen A. Mannella
    • 1
    • 2
  • Xiao Wei Guo
    • 1
  • James Dias
    • 1
    • 2
  1. 1.Wadsworth Center for Laboratories and ResearchNew York State Department of HealthAlbany
  2. 2.Department of Biomedical Sciences, School of Public HealthState University of New York at AlbanyAlbany

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