Interaction of N-acetylglutamate kinase with a PII-like protein in rice [Oryza sativa]

• Published in: Plant and cell physiology 2004-12, Vol.45 (12), p.1768-1778
• Main Authors: Sugiyama, K. (Tohoku Univ., Sendai (Japan)), Hayakawa, T, Kudo, T, Ito, T, Yamaya, T
• Format: Article
• Language: English
• Subjects: 2-OG; 2-oxoglutarate; 3-amino-1; 3AT; 4-triazole; 5-fluoroorotic acid; 5-FOA; adenylyltransferase; Amino Acid Sequence; Arabidopsis Proteins - metabolism; ATase; Base Sequence; cetyltrimethyl-ammonium bromide; Chloroplasts - genetics; Chloroplasts - metabolism; CTAB; Dig; digoxigenin; DNA, Complementary - analysis; DNA, Complementary - genetics; ENZYMES; GENE EXPRESSION; Gene Expression Regulation, Plant - genetics; GFP; glutamate synthase; Glutamates - metabolism; glutamine synthetase; GOGAT; green fluorescent protein; Keywords: N-acetylglutamate kinase — PII-like protein — Rice — Yeast two-hybrid analysis; Molecular Sequence Data; N-acetylglutamate kinase; NAGK; Oryza - genetics; Oryza - metabolism; ORYZA SATIVA; Phosphotransferases (Carboxyl Group Acceptor) - metabolism; Phosphotransferases - metabolism; PII Nitrogen Regulatory Proteins; Plant Leaves - genetics; Plant Leaves - metabolism; Plant Proteins - genetics; Plant Proteins - isolation & purification; Plant Proteins - metabolism; Plant Roots - genetics; Plant Roots - metabolism; PROTEINS; RACE; rapid amplification of cDNA ends; reverse transcription-PCR; RT-PCR; uridylyltransferase; UTase
• ISSN: 0032-0781; 1471-9053
• DOI: 10.1093/pcp/pch199

PII protein in bacteria is a sensor for 2-oxoglutarate and a transmitter for glutamine signaling. We identified an OsGlnB gene that encoded a bacterial PII-like protein in rice. Yeast two-hybrid analysis showed that an OsGlnB gene product interacted with N-acetylglutamate kinase 1 (OsNAGK1) and PII-like protein (OsGlnB) itself in rice. In cyanobacteria, NAGK is a key enzyme in arginine biosynthesis. Transient expression of OsGlnB cDNA or OsNAGK1 cDNA fused with sGFP in rice leaf blades strongly suggested that the PII-like protein as well as OsNAGK1 protein is located in chloroplasts. Both OsGlnB and OsNAGK1 genes were expressed in roots, leaf blades, leaf sheaths and spikelets of rice, and these two genes were coordinately expressed in leaf blades during the life span. Thus, PII-like protein in rice plants is potentially able to interact with OsNAGK1 protein in vivo. This finding will provide a clue to the precise physiological function of PII-like protein in rice.