Cellular localization of NADH-dependent glutamate-synthase protein in vascular bundles of unexpanded leaf blades and young grains of rice plants

Planta ◽  
1994 ◽  
Vol 193 (3) ◽  
Author(s):  
Toshihiko Hayakawa ◽  
Teiji Nakamura ◽  
Fuyu Hattori ◽  
Tadahiko Mae ◽  
Kunihiko Ojima ◽  
...  
2003 ◽  
Vol 20 (1) ◽  
pp. 43-55 ◽  
Author(s):  
Toshihiko HAYAKAWA ◽  
Takahiro SAKAI ◽  
Keiki ISHIYAMA ◽  
Naoya HIROSE ◽  
Hiroyuki NAKAJIMA ◽  
...  

Author(s):  
Keiki Ishiyama ◽  
Soichi Kojima ◽  
Toshihiko Hayakawa ◽  
Tomoyuki Yamaya

2000 ◽  
Vol 27 (9) ◽  
pp. 787 ◽  
Author(s):  
Soichi Kojima ◽  
Michiko Kimura ◽  
Yukine Nozaki ◽  
Tomoyuki Yamaya

This paper originates from a presentation at the International Conference on Assimilate Transport and Partitioning, Newcastle, NSW, August 1999 The entire 3.7 kbp 5´-upstream region (–2840 to +886) from the translational start codon of NADH–glutamate synthase (NADH–GOGAT, EC 1.4.1.14) gene from rice (Oryza sativa L.) or the region sequentially deleted from the 5´-end was fused with the β−glucuronidase (GUS) reporter gene. The chimeric gene was introduced into calli derived from rice scutellum via Agrobacterium tumefaciens-mediated transformation and tissue-specific GUS activity determined in T0 generations. When the entire region was fused, GUS activity was detected in vascular bundles of the developing leaf blade and in dorsal and lateral vascular bundles of developing grains. This corresponds with our previous immunodetection of NADH–GOGAT protein (Hayakawa et al., Planta 193, 455–460, 1994). A series of deletion experiments showed that a 149-nucleotide region between –142 and +7 was essential for promoter activity in the NADH–GOGAT gene.


1974 ◽  
Vol 43 (3) ◽  
pp. 389-401 ◽  
Author(s):  
Harunosuke KAWAHARA ◽  
Nobuo CHONAN ◽  
Toshiaki MATSUDA
Keyword(s):  

2014 ◽  
Vol 80 (16) ◽  
pp. 5043-5052 ◽  
Author(s):  
Zhihua Bao ◽  
Takashi Okubo ◽  
Kengo Kubota ◽  
Yasuhiro Kasahara ◽  
Hirohito Tsurumaru ◽  
...  

ABSTRACTIn a previous study by our group, CH4oxidation and N2fixation were simultaneously activated in the roots of wild-type rice plants in a paddy field with no N input; both processes are likely controlled by a rice gene for microbial symbiosis. The present study examined which microorganisms in rice roots were responsible for CH4oxidation and N2fixation under the field conditions. Metaproteomic analysis of root-associated bacteria from field-grown rice (Oryza sativaNipponbare) revealed that nitrogenase complex-containing nitrogenase reductase (NifH) and the alpha subunit (NifD) and beta subunit (NifK) of dinitrogenase were mainly derived from type II methanotrophic bacteria of the familyMethylocystaceae, includingMethylosinusspp. Minor nitrogenase proteins such asMethylocella,Bradyrhizobium,Rhodopseudomonas, andAnaeromyxobacterwere also detected. Methane monooxygenase proteins (PmoCBA and MmoXYZCBG) were detected in the same bacterial group of theMethylocystaceae. Because these results indicated thatMethylocystaceaemembers mediate both CH4oxidation and N2fixation, we examined their localization in rice tissues by using catalyzed reporter deposition-fluorescencein situhybridization (CARD-FISH). The methanotrophs were localized around the epidermal cells and vascular cylinder in the root tissues of the field-grown rice plants. Our metaproteomics and CARD-FISH results suggest that CH4oxidation and N2fixation are performed mainly by type II methanotrophs of theMethylocystaceae, includingMethylosinusspp., inhabiting the vascular bundles and epidermal cells of rice roots.


2000 ◽  
Vol 41 (7) ◽  
pp. 874-880 ◽  
Author(s):  
Kentaro Nakano ◽  
Tatsuro Suzuki ◽  
Toshihiko Hayakawa ◽  
Tomoyuki Yamaya

1999 ◽  
Vol 119 (2) ◽  
pp. 409-416 ◽  
Author(s):  
Toshihiko Hayakawa ◽  
Laura Hopkins ◽  
Lucy J. Peat ◽  
Tomoyuki Yamaya ◽  
Alyson K. Tobin

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