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J. Biol. Chem., Vol. 265, Issue 25, 15118-15123, Sep, 1990
P Briza, A Ellinger, G Winkler and M Breitenbach
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.
Characterization of a DL-dityrosine-containing macromolecule from yeast ascospore walls
Institut fur Allgemeine Biochemie und Ludwig-Boltzmann-Forschungsstelle fur Biochemie, Wien, Austria.
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