A mitochondrial porin cDNA predicts the existence of multiple human porins.

Academic Article


  • Pores formed in the outer membrane of mitochondria by mitochondrial porin make it permeable to water-soluble metabolites smaller than approximately 5 kDa. We have isolated a full-length cDNA encoding a human porin. This probe detects a single approximately 1.5-kilobase mRNA species on Northern blots, but multiple hybridizing bands on genomic Southern blots. The open reading frame predicts a 38.1-kDa protein with a pI of 6.59 that is homologous but not identical to a previously reported protein sequence of a 31-kDa porin isolated from human lymphocytes (porin 31HL). The most striking difference between the two porins is that the sequence predicted by the cDNA is longer than the 31HL porin by 27 amino acids at the amino terminus and 38 amino acids at the carboxyl terminus. The porin cDNA directs the in vitro translation of two protein species of approximately 32 and approximately 36 kDa, which appear to result from alternate usage of AUG initiation codons. The 32-kDa protein is the predominant species imported into both rat and yeast mitochondria in vitro. Taken together, these results suggest that multiple porin proteins can be expressed in humans. Additionally, a porin consensus protein sequence has been identified that is conserved in eukaryotic organisms as diverse as yeast and man.
  • Published In


  • Amino Acid Sequence, B-Lymphocytes, Bacterial Outer Membrane Proteins, Base Sequence, Blotting, Southern, Cell Line, Cloning, Molecular, DNA Probes, DNA, Mitochondrial, Gene Library, Humans, Ion Channels, Mitochondria, Molecular Sequence Data, Molecular Weight, Neurospora crassa, Open Reading Frames, Palatine Tonsil, Porins, Protein Biosynthesis, Protein Conformation, RNA, Messenger, Restriction Mapping, Saccharomyces cerevisiae, Sequence Homology, Amino Acid
  • Author List

  • Ha H; Hajek P; Bedwell DM; Burrows PD
  • Start Page

  • 12143
  • End Page

  • 12149
  • Volume

  • 268
  • Issue

  • 16