Mitochondria-derived and extra-mitochondrial human type-1 porin are identical as revealed by amino acid sequencing and electrophysiological characterisation

Biol Chem. 1999 Dec;380(12):1461-6. doi: 10.1515/BC.1999.189.

Abstract

In mammalian cells porin channels are localised in both mitochondrial outer membranes and extra-mitochondrial membranes. We isolated mitochondria-derived porin of a human lymphoblastoid B cell line, determined its amino acid sequence and characterised its channel properties. Interestingly, the amino acid sequence of this porin preparation and, correspondingly, its electrophysiological characteristics in a reconstituted system were identical to those of 'Porin 31HL', the human type-1 porin purified from a crude membrane preparation of the same cell line using a different purification protocol. The results raise questions about targeting, insertion and orientation of human type-1 porin in different membranes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Humans
  • Membrane Potentials / physiology
  • Molecular Sequence Data
  • Porins / chemistry*
  • Porins / physiology
  • Sequence Homology, Amino Acid
  • Voltage-Dependent Anion Channel 1
  • Voltage-Dependent Anion Channels

Substances

  • Porins
  • VDAC1 protein, human
  • Voltage-Dependent Anion Channels
  • Voltage-Dependent Anion Channel 1