Journal Article

Interaction of <i>N</i>-Acetylglutamate Kinase with a PII-Like Protein in Rice

Kenjiro Sugiyama, Toshihiko Hayakawa, Toru Kudo, Takashi Ito and Tomoyuki Yamaya

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 45, issue 12, pages 1768-1778
Published in print December 2004 | ISSN: 0032-0781
Published online December 2004 | e-ISSN: 1471-9053 | DOI:
Interaction of N-Acetylglutamate Kinase with a PII-Like Protein in Rice

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  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry


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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.

Keywords: Keywords: N-acetylglutamate kinase — PII-like protein — Rice — Yeast two-hybrid analysis.; Abbreviations: ATase, adenylyltransferase; 3AT, 3-amino-1,2,4-triazole; CTAB, cetyltrimethyl-ammonium bromide; Dig, digoxigenin; 5-FOA, 5-fluoroorotic acid; GFP, green fluorescent protein; GOGAT, glutamate synthase; GS, glutamine synthetase; NAGK, N-acetylglutamate kinase; 2-OG, 2-oxoglutarate; RACE, rapid amplification of cDNA ends; RT-PCR, reverse transcription-PCR; UTase, uridylyltransferase.

Journal Article.  7682 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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