Abstract
URF13, a mitochondrial membrane protein in maize (Zea mays L.) carrying the cms-T cytoplasm, is responsible for Texas cytoplasmic male sterility and susceptibility of cms-T maize to the fungal pathogens Cochliobolus heterostrophus race T and Mycosphaerella zeamaydis. URF13 is a ligand-gated, pore-forming receptor for the pathotoxins produced by these fungal pathogens. URF13, which contains three transmembrane α-helices, forms oligomers in cms-T maize mitochondria and when expressed in Eschericia coli cells. To study the tertiary and quaternary structure of URF13 oligomers and their interactions with the pathotoxins, we employed site-directed mutagenesis and chemical cross-linking. We determined that URF13 oligomers contain a central core of helices II. More recently, we introduced Cys residues into consecutive positions 78–82 and tested for diamide-induced cross-linking of the introduced Cys residues to Cys-27, the only Cys residue in native URF13. Our results suggest that amino acids 78–82 extend out of the membrane and into the center of the URF13 oligomers.
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References
Levings, C. S., III (1990) The Texas cytoplasm of maize: Cytoplasmic male sterility and disease susceptibility. Science 250, 942–947.
Levings, C. S., III, and Siedow, J. N. (1992) Molecular basis of disease susceptibility in the Texas cytoplasm of maize. Plant Mol. Biol. 19, 135–147.
Lim, S. M., and Hooker, A. L. (1972) Disease determinant of Helminthosporium maydis race T. Phytopathology 62, 968–971.
Kono, Y., and Daly, J. M. (1979) Characterization of the host-specific pathotoxin produced by Helminthosporium maydis, race T, affecting corn with Texas male sterile cytoplasm. Bioorg. Chem. 8, 391–397.
Danko, S. J., Kono, Y., Daly, J. M., Suzuki, Y., Takeuchi, S., and McCrery, D. A. (1984) Structure and biological activity of a host-specific toxin produced by the fungal corn pathogen Phyllosticta maydis. Biochemistry 23, 759–766.
Bednarski, M. A., Izawa, S., and Scheffer, R. P. (1977) Reversible effects of toxin from Helminthosporium maydis race T on oxidative phosphorylation by mitochondria from maize. Plant Physiol. 59, 540–545.
Bervillé, A., Ghazi, A., Charbonnier, M., and Bonavent J-F. (1984) Effects of methomyl and Helminthosporium maydis toxin on matrix volume, protonmotive force, and NAD accumulation in maize (Zea mays L.) mitochondria. Plant Physiol. 76, 508–517.
Holden, M. J., and Sze, H. (1984) Helminthosporium maydis T toxin increased membrane permeability to Ca2+ in susceptible com mitochondria. Plant Physiol. 75, 235–237.
Holden, M. J., and Sze, H. (1987) Dissipation of the membrane potential in susceptible corn mitochondria by the toxin of Helminthosporium maydis, race T, and toxin analogs. Plant Physiol. 84, 670–676.
Matthews, D. E., Gregory, P., and Gracen, V. E. (1979) Helminthosporium maydis race T toxin induces leakage of NAD+ from T cytoplasm corn mitochondria. Plant Physiol. 63, 1149–1153.
Miller, R. J., and Koeppe, D. E. (1971) Southern corn leaf blight: Susceptible and resistant mitochondria. Science 173, 67–69.
Peterson, P. A., Flavell, R. B., and Barratt, D. H. P. (1975) Altered mitochondrial membrane activities associated with cytoplasmically-inherited disease sensitivity in maize. Theor. Appl. Genet. 45, 309–314.
Klein, R. R., and Koeppe, D. E. (1985) Mode of methomyl and Bipolaris maydis (race T) toxin in uncoupling Texas male-sterile cytoplasm corn mitochondria. Plant Physiol. 77, 912–916.
Forde, B. G., Oliver, R. J. C., and Leaver, C. J. (1978) Variation in mitochondrial translation products associated with male-sterile cytoplasms in maize. Proc. Natl. Acad. Sci. U.S.A. 75, 3841–3845.
Forde, B. G., and Leaver, C. J. (1980) Nuclear and cytoplasmic genes controlling synthesis of variant mitochondrial polypeptides in male-sterile maize. Proc. Natl. Acad. Sci. U.S.A. 77, 418–422.
Dewey, R. E., Levings, C. S., III, and Timothy, D. H. (1986) Novel recombinations in the maize mitochondrial genome produce a unique transcriptional unit in the Texas male-sterile cytoplasm. Cell 44, 439–449.
Dewey, R. E., Timothy, D. H., and Levings, C. S., III (1987) A mitochondrial protein associated with cytoplasmic male sterility in the T cytoplasm of maize. Proc. Natl. Acad. Sci. U.S.A. 84, 5374–5378.
Wise, R. P., Fliss, A. E., Pring, D. R., and Gengenbach, B. G. (1987) urf13-Tof T cytoplasm maize mitochondria encodes a 13 kD polypeptide. Plant Mol. Biol. 9, 121–126.
Dewey, R. E., Siedow, J.N., Timothy, D. H., and Levings, C. S., III (1988) A 13-kilodalton maize mitochondrial protein in E. coli confers sensitivity to Bipolaris maydis toxin. Science 239, 293–295.
Braun, C. J., Siedow, J. N., Williams, M. E., and Levings, C. S., III (1989) Mutations in the maize mitochondrial T-urf13 gene eliminate sensitivity to a fungal pathotoxin. Proc. Natl. Acad. Sci. U.S.A. 86, 4435–4439.
Braun, C. J., Siedow, J. N., and Levings, C. S., III (1990) Fungal toxins bind to the URF13 protein in maize mitochondria and Escherichia coli. Plant Cell 2, 153–161.
Ojcius, D. M., and Young, J. D.-E. (1991) Cytolytic pore-forming proteins and peptides: Is there a common structural motif? Trends Biochem. Sci. 16, 225–229.
Korth, K. L., Kaspi, C. I., Siedow, J. N., and Levings, C. S., III (1991) URF13, a maize mitochondrial pore-forming protein, is oligomeric and has a mixed orientation in Escherichia coli plasma membranes. Proc. Natl. Acad. Sci. U.S.A. 88, 10865–10869.
Davidson, V. L., Brunden, K. R., Cramer, W. A., and Cohen, F. S. (1984) Studies on the mechanism of action of channel-forming colicins using artificial membranes. J. Membr. Biol. 79, 105–118.
Montai, M. (1990) Molecular anatomy and molecular design of channel proteins FASEB J 4, 2623–2635.
Kaspi, C. I., and Siedow, J. N. (1993) Cross-linking of the cms-T mitochondrial poreforming protein URF13 by N,N′-dicyclohexylcarbodiimide and its effect on URF13 sensitivity to fungal toxins. J. Biol. Chem. 268, 5828–5833.
Nałeçz, M. J., Casey, R. P., and Azzi, A. (1986) Use of N,N′-dicyclohexylcarbodiimide to study membrane-bound enzymes. Methods Enzymol. 125, 86–108.
Rhoads, D. M., Kaspi, C. I., Levings, C. S., III, and Siedow, J. N. (1994) N,N′-Dicyclohexylcarbodiimide cross-linking suggests a central core of helices II in oligomers of URF13, the pore-forming, T-toxin receptor of cms-T maize mitochondria. Proc. Natl. Acad. Sci. U.S.A. 91, 8253–8257.
Levings, C. S., III, Rhoads, D. M., and Siedow, J. N. (1995) Molecular interactions of Bipolaris maydis T-toxin and maize. Can. J. Bot. 73(Suppl. 1), S483–S489.
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Rhoads, D.M., Brunner-Neuenschwander, B., Levings, C.S., Siedow, J.N. (1998). Characterization of the Interaction Between Fungal Pathotoxins and URF13, the cms-T Maize Mitochondrial T-Toxin Receptor. In: Kohmoto, K., Yoder, O.C. (eds) Molecular Genetics of Host-Specific Toxins in Plant Disease. Developments in Plant Pathology, vol 13. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5218-1_39
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DOI: https://doi.org/10.1007/978-94-011-5218-1_39
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