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An interplay between the TOM complex and porin isoforms in the yeast Saccharomyces cerevisiae mitochondria
Author(s) -
Antos Nina,
Budzińska Malgorzata,
Kmita Hanna
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02575-3
Subject(s) - porin , saccharomyces cerevisiae , voltage dependent anion channel , gene isoform , metabolite , yeast , mitochondrion , biochemistry , ion channel , chemistry , bacterial outer membrane , microbiology and biotechnology , biophysics , biology , gene , escherichia coli , receptor
The outer mitochondrial membrane of Saccharomyces cerevisiae contains two isoforms of mitochondrial porin, known also as the voltage‐dependent anion channel. The isoform termed here porin1 displays channel‐forming activity enabling metabolite transport whereas the second one, termed here porin2, does not form a channel and its function is still not clear. We have shown recently that in the absence of porin1, the channel within the protein import machinery (the TOM complex) is essential for metabolite transport across the outer membrane [Kmita and Budzińska, Biochim. Biophys. Acta 1509 (2000) 6044–6050]. Here, we report that the TOM complex channel may also serve as a supplementary pathway for metabolites in the presence of porin1 when the permeability of the latter is limited and the role of the TOM complex seems to increase when porin2 is depleted.