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.
Membrane protein thiol cross-linking associated with the permeabilization of the inner mitochondrial membrane by Ca2+ plus prooxidants.