Characterization of a DL-dityrosine-containing macromolecule from yeast ascospore walls.

We have shown previously that the outer layers of yeast ascospore walls contain dityrosine and that this amino acid is a major component of the cross-linked peptides present in the spore wall (Briza, P., Winkler, G., Kalchhauser, H., and Breitenbach, M. (1986) J. Biol. Chem. 261, 4288-4294). We now present evidence that dityrosine is located in the outermost layer and that it is in the DL-configuration. Although the proteins (peptides) of the spore wall are insoluble, the macromolecule containing dityrosine can be solubilized by partial acid hydrolysis of spore walls. Analysis of this macromolecule indicates that it contains more than 50 mol% dityrosine and a very limited number of other amino acids. Interestingly, part of the dityrosine of spore walls is present in the DL-configuration. We speculate that not only the high degree of cross-links in the outermost layer but also the D-configuration of part of the alpha-C-atoms of dityrosine could contribute to the spores' resistance to lytic enzymes.