
Purification and Characterisation of a Pore Protein of the Outer Mitochondrial Membrane from Neurospora crassa
Author(s) -
FREITAG Helmut,
NEUPERT Walter,
BENZ Roland
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb06578.x
Subject(s) - neurospora crassa , membrane , bacterial outer membrane , translocase of the outer membrane , inner mitochondrial membrane , conductance , voltage dependent anion channel , membrane potential , biophysics , neurospora , chemistry , mitochondrial carrier , mitochondrion , lipid bilayer , porin , membrane protein , biochemistry , mitochondrial membrane transport protein , biology , gene , mathematics , escherichia coli , combinatorics , mutant
The major protein of the outer mitochondrial membrane of Neurospora was purified. On dodecylsulfate‐containing gels it displayed a single bend with an apparent molecular weight of 31000. reconstitution experiments with artifical lipid bilayers showed that this protein forms pores. Pore conductance was dependent on the voltage across the membrane. The protein inserted into the membrane in an oriented fashion, the membrane current being dependent on the sign of the voltage. Single pore conductance was 5nS, suggesting a diameter of 2nm of the open pore. This mitochondrial protein shows a number of similarities to the outer membrane porins of gram‐negative bacteria.