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Plant Physiol, November 1999, Vol. 121, pp. 1003-1015
A Transglutaminase Immunologically Related to Tissue
Transglutaminase Catalyzes Cross-Linking of Cell Wall Proteins in
Chlamydomonas reinhardtii1
Sabine
Waffenschmidt,
Thomas
Kusch, and
Jeffrey Paul
Woessner*
Institut für Biochemie (S.W., T.K.) and Institut für
Genetik (T.K.), Universität zu Köln, Köln, Germany;
and Paradigm Genetics, Research Triangle Park, North Carolina
(J.P.W.)
The addition of primary amines to the
growth medium of the unicellular green alga Chlamydomonas
reinhardtii disrupts cell wall assembly in both vegetative and
zygotic cells. Primary amines are competitive inhibitors of the
protein-cross-linking activity of transglutaminases. Two independent
assays for transglutaminase confirmed a burst of extracellular activity
during the early stages of cell wall formation in both vegetative cells
and zygotes. When non-inhibiting levels of a radioactive primary amine
(14C-putrescine) were added to the growth medium, both cell
types were labeled in a reaction catalyzed by extracellular
transglutaminase. The radioactive label was found specifically in the
cell wall proteins of both cell types, and acid hydrolysis of the
labeled material released unmodified 14C-putrescine.
Western blots of the proteins secreted at the times of maximal
transglutaminase activity in both cell types revealed a single highly
cross-reactive 72-kD band when screened with antibodies to guinea pig
tissue transglutaminase. Furthermore, the proteins immunoprecipitated
by this antiserum in vivo exhibited transglutaminase activity. We
propose that this transglutaminase is responsible for an early cell
wall protein cross-linking event that temporally precedes the oxidative
cross-linking mediated by extracellular peroxidases.
1
Financial support by the Deutsche
Forschungsgemeinschaft and the Fonds der chemischen Industrie made this
work possible.
*
Corresponding author; e-mail
jwoessner{at}paradigmgenetics.com; fax 919-544-8094.
© 1999 American Society of Plant Physiologists
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