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The Serine Proteinase Inhibitor OsSerpin Is a Potent Tillering Regulator in Rice
( Song Yion Yeu ),( Bong Soo Park ),( Wan Gyu Sang ),( Yang Do Choi ),( Min Chul Kim ),( Jong Tae Song ),( Nam Chon Paek ),( Hee Jong Koh ),( Hak Soo Seo ) 한국식물학회 2007 Journal of Plant Biology Vol.50 No.5
Tillering in rice (Oryza sativa L.) is an important agronomic trait that enhances grain production. A tiller is a specialized grainbearing branch that is formed on a non-elongated basal internode that grows independently of the mother stem. Transgenic rice over-expressing the transcription factor OsTB1, a homologue of maize TB1 (Teosinte Branched 1), exhibits markedly reduced lateral branching without the propagation of axillary buds being affected. However, the tillering mechanism remains unknown. Therefore, to further understand that mechanism, we applied proteomics methodology to isolate the proteins involved. Using two-dimensional gel electrophoresis and mass spectrometry, our analysis of the basal nodes from two rice cultivars that differ in their numbers of tillers showed that a rice serine proteinase inhibitor, OsSerpin, accumulates in great amounts in high-tillering ``Hwachung`` rice. Northern blot analysis revealed that much more OsSerpin transcript is found in ``Hwachung`` than in relatively low-tillering ``Hanmaeum``, likely because of high levels of transcription. Therefore, our data suggest that OsSerpin content determines the extent of lateral branching.
Floral Nectary-specific Gene NTR1 Encodes a Jasmonic Acid Carboxyl Methyltransferase
Seo, Hak Soo,Song, Jong Tae,Koo, Yeon Jong,Jung, Choonkyun,Yeu, Song Yion,Kim, Minkyun,Song, Sang Ik,Lee, Jong Seob,Hwang, Ingyu,Cheong, Jong-Joo,Choi, Yang Do 한국응용생명화학회 2001 Journal of Applied Biological Chemistry (J. Appl. Vol.44 No.3
NTR1 gene of Brassica campestris L. ssp. perkinensis encodes a floral nectary-specific methyltransferase. In this study, the NTR1 cDNA was expressed in E. coli to examine the enzymatic characteristics of the protein product. The GST-NTR1 fusion protein was purified to near homogeneity, showing that the size of NTR1 was 44 kDa. The protein reacted specifically with jasmonic acid (JA), consuming methyl group from S-adenosyl-L-methionine (SAM). GC-MS analysis revealed that the compound produced was authentic methyl jasmonate (MeJA), suggesting that NTR1 is an S-adenosyl-L-methionine: jasmonic acid carboxyl methyltransferase. Km values of NTR1 for JA and SAM were 38.0 and $6.4{\mu}M$, respectively. Optimal activity of the NTR1 was observed at $20^{\circ}C$, pH 7.5, in the presence of 100-150 mM KCl. Thus, kinetic properties, thermal characteristics, optimal pH, and ion-dependency of the NTR1 activity were almost identical to those of Arabidopsis JA methyltransferase JMT, indicating that these two proteins are orthologues of each other.
(Yang Do Choi,(Jong Joo Cheong,(Ing Yu Hwang,(Jong Seob Lee,(Sang Ik Song,(Min Kyun Kim,(Song Yion Yeu,(Choon Kyun Jung,(Yeon Jong Koo,(Jong Tae Song,(Hak Soo Seo 한국응용생명화학회 2001 Journal of Applied Biological Chemistry (J. Appl. Vol.44 No.3
NTR1 gene of Brassica campestris L.ssp.perkinensis encodes a floral nectary-specific methyltransferase. In this study, the NTRl cDNA was expressed in E. coli to examine the enzymatic characteristics of the protein product. The GST-NTR1 fusion protein was p