Calmodulin binding to glutamate decarboxylase is required for regulation of glutamate and GABA metabolism and normal development in plants

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Calmodulin binding to glutamate decarboxylase is required for regulation of glutamate and GABA metabolism and normal development in plants

Year: 

1996

Source of publication :

eLife

Authors :

ארזי, צחי

.

Volume :

Co-Authors: 

Baum, G., Department of Plant Genetics, Weizmann Institute of Science, 76100 Rehovot, Israel
Lev-Yadun, S., Department of Plant Genetics, Weizmann Institute of Science, 76100 Rehovot, Israel, Zinman Institute of Archeology, University of Haifa, Haifa 31905, Israel
Fridmann, Y., Department of Plant Genetics, Weizmann Institute of Science, 76100 Rehovot, Israel
Arazi, T., Department of Plant Genetics, Weizmann Institute of Science, 76100 Rehovot, Israel
Katsnelson, H., Department of Plant Genetics, Weizmann Institute of Science, 76100 Rehovot, Israel
Zik, M., Department of Plant Genetics, Weizmann Institute of Science, 76100 Rehovot, Israel
Fromm, H., Department of Plant Genetics, Weizmann Institute of Science, 76100 Rehovot, Israel

From page: 

2988

To page: 

2996

(

Total pages: 

9

)

Link :

Calmodulin binding to glutamate decarboxylase is required for regulation of glutamate and GABA metabolism and normal development in plants

Abstract: 

Glutamate decarboxylase (GAD) catalyzes the decarboxylation of glutamate to CO2 and γ-aminobutyrate (GABA). GAD is ubiquitous in prokaryotes and eukaryotes, but only plant GAD has been shown to bind calmodulin (CaM). Here, we assess the role of the GAD CaM-binding domain in vivo. Transgenic tobacco plants expressing a mutant petunia GAD lacking the CaM-binding domain (GADΔC plants) exhibit severe morphological abnormalities, such as short stems, in which cortex parenchyma cells fail to elongate, associated with extremely high GABA and low glutamate levels. The morphology of transgenic plants expressing the full-length GAD (GAD plants) is indistinguishable from that of wild-type (WT) plants. In WT and GAD plant extracts, GAD activity is inhibited by EGTA and by the CaM antagonist trifluoperazine, and is associated with a CaM-containing protein complex of ~ 500 kDa. In contrast, GADΔC plants lack normal GAD complexes, and GAD activity in their extracts is not affected by EGTA and trifluoperazine. We conclude that CaM binding to GAD is essential for the regulation of GABA and glutamate metabolism, and that regulation of GAD activity is necessary for normal plant development. This study is the first to demonstrate an in vivo function for CaM binding to a target protein in plants.