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J. Biol. Chem., Vol. 269, Issue 42, 26402-26410, 10, 1994
L Heins, H Mentzel, A Schmid, R Benz and UK Schmitz
The mitochondrial outer membrane of eukaryotic cells contains a voltage-
dependent anion channel termed porin. In the organisms studied so far only
one type of porin has been identified at the protein level. Here we present
a biochemical and molecular genetic analysis of two different porin
polypeptides of M(r) 34,000 and 36,000 from the outer membranes of potato
mitochondria (termed POM 34 and POM 36, respectively). N-terminal
sequencing and the use of labeled oligonucleotide mixtures derived from
these amino acid sequences allowed the isolation of cDNA clones encoding
the 34- and 36-kDa proteins. They have similar steady state protein levels
and share about 75% identical amino acids suggesting that they represent
isoforms. In addition, a third cDNA clone coding for a slightly different
isoform of the 36-kDa protein was characterized. The polypeptides encoded
by the three cDNA clones share the highest degree of sequence identity with
mitochondrial porins from fungi and mammals. Tentative models of the
secondary structure of the 34- and 36-kDa proteins suggest the occurrence
of a 16-stranded beta-barrel typical for bacterial and mitochondrial
porins. Purification of the 34-kDa protein by hydroxyapatite chromatography
allowed conductance measurements in artificial bilayers. The 34-kDa protein
is a voltage-dependent, channel- forming component with single channel
conductances of 3.5 and 2.0 nanosiemens in 1 M KCl. In spite of the
striking functional similarities to mitochondrial porins from other
organisms neither the 34- nor the 36-kDa proteins are able to complement
the respiratory defect of a yeast por- mutant.
Biochemical, molecular, and functional characterization of porin isoforms from potato mitochondria
Institut fur Genbiologische Forschung Berlin GmbH, Federal Republic of Germany.
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