Ca2+-Independent Permeabilization of the Inner Mitochondrial Membrane by Peroxynitrite Is Mediated by Membrane Protein Thiol Cross-Linking and Lipid Peroxidation

1997 ◽  
Vol 345 (2) ◽  
pp. 243-250 ◽  
Author(s):  
F.R. Gadelha ◽  
L. Thomson ◽  
M.M. Fagian ◽  
A.D.T. Costa ◽  
R. Radi ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Membrane Protein ◽  
Mitochondrial Membrane ◽  
Cross Linking ◽  
Inner Mitochondrial Membrane ◽  
Protein Thiol

scholarly journals A Multisubunit Complex of Outer and Inner Mitochondrial Membrane Protein Translocases Stabilizedin Vivoby Translocation Intermediates

1999 ◽  
Vol 274 (32) ◽  
pp. 22847-22854 ◽  
Author(s):  
Norbert Schülke ◽  
Naresh Babu V. Sepuri ◽  
Donna M. Gordon ◽  
Sandeep Saxena ◽  
Andrew Dancis ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Mitochondrial Membrane ◽  
Inner Mitochondrial Membrane ◽  
Mitochondrial Membrane Protein

Molecular interactions of Bipolaris maydis T-toxin and maize

1995 ◽  
Vol 73 (S1) ◽  
pp. 483-489 ◽  
Author(s):  
Charles S. Levings III ◽  
David M. Rhoads ◽  
James N. Siedow
Keyword(s):  
Male Sterility ◽  
Mitochondrial Membrane ◽  
Fungal Pathogens ◽  
Mitochondrial Gene ◽  
Site Directed Mutagenesis ◽  
Cross Linking ◽  
Male Sterile ◽  
Inner Mitochondrial Membrane ◽  
Bipolaris Maydis ◽  
Maize Cytoplasmic Male Sterility

The toxins (T-toxins) produced by the fungal pathogens Bipolaris maydis race T (BmT) and Phyllosticta maydis (Pm) target the mitochondrial receptor, URF13, in maize (Zea mays L.) plants containing the Texas male-sterile cytoplasm (cms-T). URF13, a 13-kDa protein, is the product of the maize mitochondrial gene T-urf13, which is found only in the mitochondrial genome of cms-T maize and is thought to be responsible for cytoplasmically inherited male sterility and disease susceptibility. Pm-toxin binds specifically to URF13 in a cooperative manner, and Pm- and BmT-toxins compete for the same, or overlapping, binding sites. The binding of T-toxin to URF13 causes rapid permcabilization of the inner mitochondrial membrane, which results in leakage of NAD+ and other ions from the matrix. A pore consisting of at least six transmembrane α-helices is required for NAD+ leakage. Cross-linking experiments showed that URF13 oligomers are present in the mitochondrial membrane. A model of the secondary structure of URF13 proposes that each monomer contains three transmembrane α-helices. Studies combining site-directed mutagenesis and chemical cross-linking of URF13 expressed by Escherichia coli cells indicate that the oligomers are composed of a central core of helices II that line the center of the URF13 pores. Key words: maize cytoplasmic male sterility, URF13, mitochondrial pores, T-toxin receptor, Bipolaris maydis race T, Phyllosticta maydis, Helminthosporium maydis.

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