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The Foldback Intercoil Structure of pBR322 DNA Induced by a Novel Pearl Millet Mitochondrial Enzyme
김병동,임용표,Kim, Byung-Dong,Lim, Yong-Pyo Korean Society for Biochemistry and Molecular Biol 1989 한국생화학회지 Vol.22 No.1
pBR 322 DNA의 foldback intercoil 구조가 우리가 최근 진주조 마이토콘드리아에서 분리한 한 효소에 의해 유기되었다. 독특한 DNA 형태들, 즉 올가미, stem, loop, stem-and-loop 등이 선형과 원형 pBR322에서 효소에 의해 형성된다는 사실로 보아 이전에 진주조 마이토콘드리아 DNA에서 발견된 동일한 형태들이 artifact가 아니었음을 입증한다. 또한, 중요한 것은, intercoil DNA와 supercoil DNA가 전자현미경 방법으로 분명히 분별될 수 있음을 보여주었다. 우리는 이 진주조 마이토콘드리아 단백질을 "synaptase" (접합효소)로 부르기를 제안하는데, 이는 이 효소가 분자내 그리고 분자간에 두개의 이중나선 DNA의 접합을 유기하기 때문이다. The foldback intercoil structure of pBR322 DNA was induced by an enzyme which we have recently isolated from pearl millet mitochondria. The enzymatic formation of the unique configurations, namely, the lasso, the stem, the loop, and the stem-and-loop on both the linear and the open circle pBR322 DNA effectively argues that the same configurations found earlier in the native pearl millet mtDNA were not artifacts. Most important, it was demonstrated that the intercoil DNA and the supercoil DNA can be resolved by the electron microscopy. We propose to call the pearl millet mitochondrial protein, "the synaptase", since it induces intra- and inter-molecular synapsis of two double helical DNA strands.
진주조 마이토콘드리아의 새로운 효소에 의해 유기된 pBR 322 DNA 의 foldback intercoil 구조
김병동,임용표 ( Byung Dong Kim,Yong Pyo Lim ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.1
The foldback intercoil structure of pBR322 DNA was induced by an enzyme which we have recently isolated from pearl millet mitochondria. The enzymatic formation of the unique configurations, namely, the lasso, the stem, the loop, and the stem-and-loop on both the linear and the open circle pBR322 DNA effectively argues that the same configurations found earlier in the native pearl millet mtDNA were not artifacts. Most important, it was demonstrated that the intercoil DNA and the supercoil DNA can be resolved by the electron microscopy. We propose to call the pearl millet mitochondrial protein, $quot;the synaptase$quot;, since it induces intra- and inter-molecular synapsis of two double helical DNA strands.
Isolation and Characterization of a DNA-binding Protein from Pearl Millet Mitochondria
임용표,김병동,Lim, Yong-Pyo,Kim, Byung-Dong 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.4
한 DNA-결합 단백질이 진주조 (Pennisetum typhoides)의 미토콘드리아 DNA로부터 분리되었다. 그 DNA결함 단백질은 negatively supercoiled pBR322 DNA를 open circle DNA를 주산물로, linear DNA와 고분자량 multimer를 부산물로 전환시켰다. 반응은 이가 양이온 ($Mg^{++}$, $Mn^{++}$, $Zn^{++}$, $Co^{++}$)을 필요하였으나 ATP를 필요로 하지 않았다. 효소반응은 고농도의 일가 및 이가 양이온, EDTA, SDS, 그리고 spermidine에 의하여 억제되었다. 이 다기능 효소 (topoisomerase, recombinase)는 박테리아 topoisomerase I과는 달리 사다리 중간물질을 만들지 않으므로 잠정적으로 신종의 topoisomerase로 명명한다. A DNA-binding protein was isolated from pearl millet (Pennisetum typhoides) mitochondrial DNA. The DNA-binding protein transformed negatively supercoiled pBR322 DNA into an open circle DNA as a major product, and a linear DNA and a high molecular weight multimer as minor products. The reaction was dependent on divalent cations ($Mg^{++}$, $Mn^{++}$, $Zn^{++}$, $Co^{++}$), but was independent of ATP. The enzyme reaction was inhibited by high concentrations of monovalent and divalent cations, EDTA, SDS, and spermidine. The putative multifunctional enzyme is tentatively designated as a new class of topoisomerase, since, unlike the bacterial topoisomerase I. it does not produce the ladder intermediates
임용표,김병동,Lim, Yong-Pyo,Kim, Byung-Dong 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.4
한 독특한 DNA-수정 효소가 진주조(Pennisetum typhoides) 미토콘드리아에서 분리되었다. 이 효소는 negatively supercoiled pBR322 DNA를 이완시켜 open circular DNA를 주산물로, 또한 linear DNA와 고분자량 multimer complex를 부산물로 만든다. 이 효소는 미토콘드리아의 용성분획에서 DEAE-cellulose 및 Sephacryl S200 SF column chromatography, 그리고 polyacrylamide gel electrophoresis에 의하여 분리되었다. 이 효소는 이가 양이온들 ($Mg^{++}$, $Mn^{++}$, $Zn^{++}$, $Co^{++}$ 및 $Ca^{++}$)을 필요로 하나 ATP는 필요로 하지 않는다. 이 효소는 고농도의 일가 몇 이가 양이온들, EDTA, SDS, 그리고 spermidine에 의해 억제된다. 이 효소의 분자량은 약 70,000으로 추정된다. 이 효소는 박테리아의 topoisomerase I과는 달리 사다리 중간산물을 만들지 않으며, 고분자량 multimer도 생산하므로 topoisomerase와 recombinase의 복합기능 단백질로 추정된다. 이 독특한 효소를 잠정적으로 "신종 토포아이소머레이즈"라 명명한다. A unique DNA-modifying enzyme has been isolated from pearl millet (Pennisetum typhoides) mitochondria. The enzyme relaxes negatively supercoiled pBR322 into an open circular DNA as a major product and also produces a linear DNA and high molecular weight multimer complexes as minor products. The enzyme was isolated from the soluble fraction of mitochondria by DEAE-cellulose and Sephacryl S200 SF column chromatography steps and polyacrylamide gel electrophoresis. The enzyme is dependent on divalent cations ($Mg^{++}$, $Mn^{++}$, $Zn^{++}$, $Co^{++}$, and $Ca^{++}$), and is independent of ATP. The enzyme is inhibited by high concentrations of monovalent and divalent cations, EDTA, SDS, and spermidine. The molecular weight of this protein is estimated to be about 70,000. The new enzyme, unlike the bacterial topoisomerase I, does not produce ladder intermediate, but also produces high molecular weight multimers. This suggests that the new protein is a mixed functional enzyme of topoisomerase and recombinase. We tentatively call this unique enzyme a novel c1ass of topoisomerase.
진주조 미토콘드리아 용성분획의 신종 토포아이소머레이즈 그의 분리와 동정
임용표,김병동 ( Yong Pyo Lim,Byung Dong Kim ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.4
A unique DNA-modifying enzyme has been isolated from pearl millet (Pennisetum typhoides) mitochondria. The enzyme relaxes negatively supercoiled pBR322 into an open circular DNA as a major product and also produces a linear DNA and high molecular weight multimer complexes as minor products. The enzyme was isolated from the soluble fraction of mitochondria by DEAE-cellulose and Sephacryl S200 SF column chromatography steps and polyacrylamide gel electrophoresis. The enzyme is dependent on divalent cations (Mg^(++), Mn^(++), Zn^(++), Co^(++), and Ca^(++)), and is independent of ATP. The enzyme is inhibited by high concentrations of monovalent and divalent cations, EDTA, SDS, and spermidine. The molecular weight of this protein is estimated to be about 70,000. The new enzyme, unlike the bacterial topoisomerase I, does not produce ladder intermediate, but also produces high molecular weight multimers. This suggests that the new protein is a mixed functional enzyme of topoisomerase and recombinase. We tentatively call this unique enzyme a novel class of topoisomerase.
진주조 미토콘드리아로 부터 DNA 결합 단백질의 분리와 동정
임용표,김병동 ( Yong Pyo Lim,Byung Dong Kim ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.4
A DNA-binding protein was isolated from pearl millet (Pennisetum typhoides) mitochondrial DNA. The DNA-binding protein transformed negatively supercoiled pBR322 DNA into an open circle DNA as a major product, and a linear DNA and a high molecular weight multimer as minor products. The reaction was dependent on divalent cations (Mg ^(++), Mn^(++), Zn^(++), and Co^(++), but was independent of ATP. The enzyme reaction was inhibited by high concentrations of monovalent and divalent cations, EDTA, SDS, and spermidine. The putative multifunctional enzyme is tentatively designated as a new class of topoisomerase, since, unlike the bacterial topoisomerase I, it does not produce the ladder intermediates.
Introduction and transposition of maize controlling element “Ac” into nicotiana tabacum
김신제(Shin Je Kim),조화진(Hwa Jin Cho),최광태(Kwang Tae Choi),임용표(Yong Pyo Lim),김병동(Byung Dong Kim) 한국육종학회 1991 한국육종학회지 Vol.23 No.1
Maize controlling element Ac was introduced into Nicotiana tabacum cv. NC82 which is cultivated widely in Korea. Agrobacterium-mediated transformation method was applied to transfer the Ac, and the transformants were regenerated to whole plants. After 2-3 weeks of inoculation of the leaf discs with Agrobacterium containing the TAc7 plasmid, callus was formed in callus inducing media supplemented with 100mg/l kanamycin. The shoots were regenerated from calli by shoot inducing media supplemented with 100mg/l kanamycin. Transformation of the regenerated plants were confirmed by checking the stability on media supplemented with kanamycin. Integration, copy number, and transposition of the Ac element in the transgenic plants were confirmed by Southern blot analysis. Five analyzed transformants contained the Ac fragments, two of which were found transposed in the plant genome.