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Purification and Characterization of Chloroplast Fructose-1,6-bisphosphatase from Pea Leaves
부성희,한태룡,Bhoo, Seong-Hee,Hahn, Tae-Ryong 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.4
엽록체 fructose-1,6-bisphosphatase를 완두 잎으로부터 1,300배 정제하였다. 정제된 효소는 거의 순수하였고 SDS polyacrylamide 전기영동하여 얻은 monomer의 분자량은 약 40,000이었다. 효소는 pH 7.5에서 활성이 없었으나 dithiothreitol 혹은 알카리 pH에서 활성화가 되었다. 이 결과는 분리된 fructose-1,6-bisphosphatase가 엽록체로부터 얻어진 것임을 나타낸다. Fructose-1,6-phosphate와 $Mg^{++}$에 대한 효소 포회곡선은 Hill 상수 2.6 및 3.1을 가진 sigmoidal한 모양을 보여주는데 이는 효소가 multimer로 구성된 allosteric 한 것임을 알 수 있다. 최고 활성의 반에 요구되는 기질농도는 $40{\mu}M$로서 이는 시금치 엽록체 효소에 대한 $80{\mu}M$값 (Zimmermann et al., 1976)보다 작았다. Chloroplast fructose-1,6-bisphosphatase was purified 1,300 fold from pea leaves. The purified enzyme appeared homogeneous and the approximate molecular weight of the monomer was 40,000, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme was inactive at pH 7.5, while it was activated by dithiothreitol or alkaline pH, indicating that the purified fructose-1,6-bisphosphatase was originated from chloroplast. The enzyme saturation curves with fructose-1,6-bisphosphate and $Mg^{++}$ show sigmoidal shapes with almost same Hill coefficients (2.6 and 3.1, respectively), suggesting that the enzyme is composed of multimer. The substrate concentration required for half-maximal activity was $40{\mu}M$ which is a comparable value $(80{\mu}M)$ for spinach chloroplast fructose bisphosphatase (Zimmermann et al., 1976).
완두엽록체 fructose - 1 , 6 - bisphosphatase 의 분리정제 및 특성
부성희,한태룡 ( Seong Hee Bhoo,Tae Ryong Hahn ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.4
Chloroplast fructose-1,6-bisphosphatase was purified 1,300 fold from pea leaves. The purified enzyme appeared homogeneous and the approximate molecular weight of the monomer was 40,000, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The enzyme was inactive at pH 7.5, while it was activated by dithiothreitol or alkaline pH, indicating that the purified fructose-1,6-bisphosphatase was originated from chloroplast. The enzyme saturation curves with fructose-1,6-bisphosphate and Mg^(++) show sigmoidal shapes with almost same Hill coefficients (2.6 and 3.1, respectively), suggesting that the enzyme is composed of multimer. The substrate concentration required for half-maximal activity was 40 μM which is a comparable value (80μM) for spinach chloroplast fructose bisphosphatase (Zimmermann et al., 1976).
생화학,분자생물학 : DEB 처리에 의해 유도된 벼 돌연변이 집단으로부터 도열병 감수성 돌연변이 분리
김혜경 ( Hye Kyung Kim ),이상규 ( Sang Kyu Lee ),한무호 ( Mu Ho Han ),전용희 ( Yong Hee Jeon ),이기환 ( Gi Hwan Yi ),이윤형 ( Youn Hyung Lee ),부성희 ( Seong Hee Bhoo ),한태룡 ( Tae Ryong Hahn ),전종성 ( Jong Seong Jeon ) 한국응용생명화학회 2005 Applied Biological Chemistry (Appl Biol Chem) Vol.48 No.4
Characterization of Rice Mutants with Enhanced Susceptibility to Rice Blast
김혜경,전종성,이상규,조정일,Sichul Lee,안진흥,Nam-Soo Jwa,Byung-Ryun Kim,Young-Chan Cho,Seong-Sook Han,Seong-Hee Bhoo,이윤형,Yeon-Kyu Hong,이기환,Dae-Sup Park,한태룡 한국분자세포생물학회 2005 Molecules and cells Vol.20 No.3
As a first step towards identifying genes involving in the signal transduction pathways mediating rice blast resistance, we isolated 3 mutants lines that showed enhanced susceptibility to rice blast KJ105 (91-033) from a T-DNA insertion library of the japonica rice cultivar, Hwayeong. Since none of the susceptible phenotypes co-segregated with the T-DNA insertion weadapted a map-based cloning strategy to isolate the gene(s) responsible for the enhanced susceptibility of the Hwayeong mutants. A genetic mapping population was produced by crossing the resistant wild type Hwayeong with the susceptible cultivar, Nagdong. Chisquare analysis of the F2 segregating population indicated that resistance in Hwayeong was controlled by a single major gene that we tentatively named Pi-hy. Randomly selected susceptible plants in the F2 population were used to build an initial map of Pi-hy. The SSLP marker RM2265 on chromosome 2 was closely linked to resistance. High resolution mapping using 105 F2 plants revealed that the resistance gene was tightly linked, or identical, to Pib, a resistance gene with a nucleotide binding sequence and leucine-rich repeats (NB-LRR) previously isolated. Sequence analysis of the Pib locus amplified from three susceptiblemutants revealed lesions within this gene, demonstrating that the Pi-hy gene is Pib. The Pib mutations in 1D- 22-10-13, 1D-54-16-8, and 1C-143-16-1 were, respectively,a missense mutation in the conserved NB domain 3, anonsense mutation in the 5th LRR, and a nonsense mutation in the C terminus following the LRRs that causes a small deletion of the C terminus. These findingsprovide evidence that NB domain 3 and the C terminus are required for full activity of the plant R gene. They also suggest that alterations of the resistance gene can cause major differences in pathogen specificity by affecting interactions with an avirulence factor.