PMID: 9163912May 1, 1997Paper

A putative role for calmodulin in the activation of Neurospora crassa chitin synthase

FEMS Microbiology Letters
K Suresh, C Subramanyam

Abstract

The possible role of calmodulin in cell wall formation and chitin synthesis was studied in Neurospora crassa by examining the effects of anti-calmodulin agents on protoplast regeneration and possible associations between chitin synthase and calmodulin related proteins in microsomal isolates. Protoplast regeneration was inhibited by trifluoperazine (> 20 microM), an anticalmodulin agent. Chitin synthase activity in microsomes was associated with that of calmodulin-dependent protein kinase and inhibited by trifluoperazine (100 microM). In vitro activity of chitin synthase was enhanced upon inclusion of calmodulin (300 ng) in the assay mix, 63% over and above the stimulation brought about by trypsin, an activator of the enzyme. Autoradiography studies on microsomal proteins revealed calmodulin-dependent phosphorylation of two microsomal calmodulin-binding proteins (106 and 89 kDa). The results indicate that calmodulin-mediated phosphorylation of specific microsomal proteins may be important in the in vivo activation of chitin synthase.

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