ABSTRACT
An Arabidopsis mutant (rnc1) with a mutation at the 313th nucleotide from the translational start site of AtNRT3.1 was isolated. The mutation resulted in the replacement of aspartate by asparagine at the 105th amino acid in a region conserved among higher plants. In the rnc1 mutant, both the nitrate concentrations in plants and the nitrate uptake from the medium were <13% compared with those of the wild type, while AtNRT3.1 mRNA was accumulated similarly and both AtNRT1.1 and AtNRT2.1 mRNA were decreased. These results suggest that the replacement of Asp105 in AtNRT3.1 markedly reduces nitrate uptake and accumulation.
Subject(s)
Anion Transport Proteins/genetics , Arabidopsis Proteins/genetics , Arabidopsis/genetics , Genes, Plant , Nitrates/metabolism , Amino Acid Sequence , Anion Transport Proteins/metabolism , Arabidopsis/metabolism , Arabidopsis Proteins/metabolism , Asparagine/genetics , Gene Expression Regulation, Plant , Molecular Sequence Data , Mutation , Plant Roots , Plants, Genetically ModifiedABSTRACT
The expression of asparagine synthetase (AS; EC 6.3.5.4) in response to externally supplied nitrogen was investigated with respect to enzyme activity and protein levels as detected immunologically in rice (Oryza sativa) seedlings. The asparagine content was very low in leaves and roots of nitrogen-starved rice plants but increased significantly after the supply of 1 mM NH4+ to the nutrient solution. While neither AS activity nor AS protein could be detected in leaves and roots prior to the supply of nitrogen, levels became detectable in roots but not in leaves within 12 h of the supply of 1 mM NH4+ or 10 mM glutamine. Other nitrogen compounds, such as nitrate, glutamate, aspartate and asparagine had no effect. Methionine sulfoximine completely inhibited the NH4+-induced accumulation of AS protein but did not affect the glutamine-induced accumulation of the enzyme. The results suggested that glutamine or glutamine-derived metabolites regulate AS expression in rice roots.
