JXB Advance Access originally published online on July 1, 2003
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Journal of Experimental Botany, Vol. 54, No. 389, pp. 2001-2002,
August 1, 2003
© 2003 Oxford University Press
Calcium/calmodulin activation of two divergent glutamate decarboxylases from tobacco*
Received 30 April 2003; Accepted 7 May 2003
,
Department of Plant Agriculture, Biotechnology Division, Bovey Building, University of Guelph, Guelph, Ontario, Canada N1G 2W1
* The nucleotide sequences for NtGAD1 and NtGAD3 were deposited in the GenBank database under the accession numbers AAK18620 and AAK38667, respectively.
To whom correspondence should be addressed. Fax: +519 767 0755. E-mail: bshelp{at}uoguelph.ca
Glutamate decarboxylase (GAD, EC 4.1.1.15
Key words: cDNA sequences,
This article has been cited by other articles:
-decarboxylation of glutamate to produce
-aminobutyrate (GABA). The nucleotide sequences of two divergent GADs (designated GAD1 and GAD3) were isolated from a Nicotiana tabacum L. cv. Samsun NN leaf cDNA library. Open reading frames indicated that GAD1 encodes a polypeptide of 496 amino acids and has greater than 99% identity with known tobacco GADs, whereas GAD3 encodes a polypeptide of 491 amino acids and has about 14% divergence from known tobacco GADs. Genomic DNA analysis suggested that there are at least four tobacco GAD genes, existing in pairs of highly identical genes. An in vitro assay at pH 7.3 revealed that activities of the recombinant proteins, after isolation from Escherichia coli and partial purification by nickel-affinity chromatography, are 57133 times the control levels in the presence of 0.5 mM calcium and 0.2 µM bovine calmodulin.
-aminobutyrate, glutamate decarboxylase, recombinant protein, tobacco.![]()
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K. Akama and F. Takaiwa
C-terminal extension of rice glutamate decarboxylase (OsGAD2) functions as an autoinhibitory domain and overexpression of a truncated mutant results in the accumulation of extremely high levels of GABA in plant cells
J. Exp. Bot.,
July 1, 2007;
58(10):
2699 - 2707.
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