An interplay between the TOM complex and porin isoforms in the yeast Saccharomyces cerevisiae mitochondria

FEBS Letters

Kmita, Hanna¹  Antos, Nina¹  Budzińska, Malgorzata¹ 

[1] Institute of Molecular Biology and Biotechnology, Department of Bioenergetics, Adam Mickiewicz University, Fredry 10, 61-701 Poznan, Poland

关键词: TOM complex;    Mitochondrial porin isoform;    Metabolite transport;    DHFR;    dihydrofolate reductase;    MOPS;    4-morpholinopropanesulfonic acid;    TOM;    translocase of the outer membrane;    VDAC;    voltage-dependent anion-selective channel;   

DOI  :  10.1016/S0014-5793(01)02575-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown