- Information
- Symbol: OsGAD2
- MSU: LOC_Os04g37500
- RAPdb: Os04g0447800
- Publication
- Rice Oryza sativa contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus, 2001, Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression.
- Seed-specific expression of truncated OsGAD2 produces GABA-enriched rice grains that influence a decrease in blood pressure in spontaneously hypertensive rats, 2009, Transgenic Res.
- 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, 2007, J Exp Bot.
- Genbank accession number
- Key message
- RNA analysis showed that transcripts of OsGAD1 and OsGAD2 were present in all tissues examined, but their expression was differentially regulated, at least in roots and maturing seeds
- We have isolated full-length cDNAs for two distinct isoforms of glutamate decarboxylase (GAD), designated OsGAD1 and OsGAD2 from a rice shoot cDNA library
- Regenerated OsGAD2DeltaC rice plants had aberrant phenotypes such as dwarfism, etiolated leaves, and sterility
- Seed-specific expression of truncated OsGAD2 produces GABA-enriched rice grains that influence a decrease in blood pressure in spontaneously hypertensive rats
- Connection
- OsGAD1, OsGAD2, Rice Oryza sativa contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus, We have isolated full-length cDNAs for two distinct isoforms of glutamate decarboxylase (GAD), designated OsGAD1 and OsGAD2 from a rice shoot cDNA library
- OsGAD1, OsGAD2, Rice Oryza sativa contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus, Open reading frames found in OsGAD1 and OsGAD2 cDNAs encode putative proteins of 501 (56
- OsGAD1, OsGAD2, Rice Oryza sativa contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus, Interestingly, in the regions in the putative gene products corresponding to the C-terminal 30-amino-acid peptide known as the calmodulin-binding domain of plant GADs, OsGAD1 possesses a typical motif, while OsGAD2 contains several substitutions of amino acids that contribute strongly to the binding of calmodulin (CaM)
- OsGAD1, OsGAD2, Rice Oryza sativa contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus, An in vitro CaM-binding assay of these proteins over-expressed in Escherichia coli revealed that OsGAD1 can in fact bind specifically to bovine CaM but OsGAD2 cannot
- OsGAD1, OsGAD2, Rice Oryza sativa contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus, RNA analysis showed that transcripts of OsGAD1 and OsGAD2 were present in all tissues examined, but their expression was differentially regulated, at least in roots and maturing seeds
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