Characterization of the Interaction Between Fungal Pathotoxins and URF13, the cms-T Maize Mitochondrial T-Toxin Receptor View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1998

AUTHORS

D. M. Rhoads , B. Brunner-Neuenschwander , C. S. Levings , J. N. Siedow

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. More... »

PAGES

355-365

Book

TITLE

Molecular Genetics of Host-Specific Toxins in Plant Disease

ISBN

978-94-010-6197-1
978-94-011-5218-1

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-94-011-5218-1_39

DOI

http://dx.doi.org/10.1007/978-94-011-5218-1_39

DIMENSIONS

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