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THE PLANT CELL, Vol 5, Issue 7 809-820, Copyright © 1993 by American Society of Plant Biologists
Isodityrosine Cross-Linking Mediates Insolubilization of Cell Walls in Chlamydomonas
S. Waffenschmidt, J. P. Woessner, K. Beer and U. W. Goodenough
Institut fur Biochemie, Universitat zu Koln, Koln, Germany
Enzymatic removal of the cell wall induces vegetative Chlamydomonas
relnhardtll cells to transcribe wall genes and synthesize new
hydroxyproline-rich glycoproteins (HRGPs) related to the extensins found in
higher plant cell walls. A cDNA expression library made from such induced
cells was screened with antibodies to an ollgopeptide containing the (SP)x
repetitive domains found in Chlamydomonas wall proteins. One of the
selected cDNAs encodes an (SP)x-rich polypeptide that also displays a
repeated YGG motif. Ascorbate, a peroxidase inhibitor, and tyrosine
derivatives were shown to inhibit insolubilization of both the vegetative
and zygotic cell walls of Chlamydomonas, suggesting that oxidative
cross-linking of tyrosines is occurring. Moreover, insolubilization of both
walls was concomitant with a burst in H2O2 production and in extracellular
peroxidase activity. Finally, both isodityrosine and dityrosine were found
in hydrolysates of the insolubilized vegetative wall layer. We propose that
the formation of tyrosine cross-links is essential to Chlamydomonas HRGP
insolubilization.
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