http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
오늘 본 자료
Baek, Kwangryul,Lee, Yew,Nam, Onyou,Park, Seunghye,Sim, Sang Jun,Jin, EonSeon WILEY‐VCH Verlag 2016 BIOTECHNOLOGY JOURNAL Vol.11 No.3
<P><B>Abstract</B></P><P>Promoter of the light‐inducible protein gene (<I>LIP</I>) of <I>Dunaliella</I> was recently isolated in our laboratory. The aim of this work is to find the light‐inducible motif in the <I>Dunaliella LIP</I> promoter and verify its regulatory motif with a <I>Gaussia</I> luciferase reporter gene transformed in <I>Chlamydomonas reinhardtii</I>. 400 bp upstream to the translational start site of the <I>Dunaliella LIP</I> gene was gradually truncated and analyzed for the luciferase expression. Furthermore, this promoter comprising duplicated or triplicated light‐responsive motifs was tested for its augmentation of light response. Two putative light‐responsive motifs, GT‐1 binding motif and sequences over‐represented in light‐repressed promoters (SORLIP) located in the 200 bp <I>LIP</I> promoter fragment were analyzed for their light responsibility. It is turned out that SORLIP was responsible for the light‐inducible activity. With the copy number of SORLIP up to three showed stronger high light response compared with the native <I>LIP</I> promoter fragment. Therefore, we found a light‐responsive DNA motif operating in <I>Chlamydomonas</I> and confirm a synthetic promoter including this motif displayed light inducibility in heterologously transformed green algae for the first time. This light‐inducible expression system will be applied to various area of algal research including algal biotechnology.</P>
Jeong, Jooyeon,Baek, Kwangryul,Yu, Jihyeon,Kirst, Henning,Betterle, Nico,Shin, Woongghi,Bae, Sangsu,Melis, Anastasios,Jin, EonSeon Oxford University Press 2018 Journal of experimental botany Vol.69 No.5
<▼1><P>The <I>Chlamydomonas reinhardtii</I> LTD null mutant generated by CRISPR–Cas9, displayed aberrant PSI–LHCI holocomplexes, suggesting that the LTD protein may selectively function in PSI–LHCI assembly in green microalgae</P></▼1><▼2><P><B>Abstract</B></P><P>Nuclear-encoded light-harvesting chlorophyll- and carotenoid-binding proteins (LHCPs) are imported into the chloroplast and transported across the stroma to thylakoid membrane assembly sites by the chloroplast signal recognition particle (CpSRP) pathway. The LHCP translocation defect (LTD) protein is essential for the delivery of imported LHCPs to the CpSRP pathway in <I>Arabidopsis</I>. However, the function of the LTD protein in <I>Chlamydomonas reinhardtii</I> has not been investigated. Here, we generated a <I>C. reinhardtii ltd</I> (<I>Crltd</I>) knockout mutant by using CRISPR–Cas9, a new target-specific knockout technology. The <I>Crltd1</I> mutant showed a low chlorophyll content per cell with an unusual increase in appressed thylakoid membranes and enlarged cytosolic vacuoles. Profiling of thylakoid membrane proteins in the <I>Crltd1</I> mutant showed a more severe reduction in the levels of photosystem I (PSI) core proteins and absence of functional LHCI compared with those of photosystem II, resulting in a much smaller PSI pool size and diminished chlorophyll antenna size. The lack of CrLTD did not prevent photoautotrophic growth of the cells. These results are substantially different from those for Arabidopsis <I>ltd</I> null mutant, indicating LTD function in LHCP delivery and PSI assembly may not be as stringent in <I>C. reinhardtii</I> as it is in higher plants.</P></▼2>
Jeon, Hancheol,Jeong, Jooyeon,Baek, Kwangryul,McKie-Krisberg, Zaid,Polle, Jü,rgen E.W.,Jin, EonSeon Elsevier 2016 Algal research Vol.19 No.-
<P><B>Abstract</B></P> <P> <I>Dunaliella salina</I> is a unicellular halophilic green alga, which can survive even in saturated brine solutions (up to 5.0M NaCl). In <I>D. salina</I>, the carbonic anhydrase (CA, EC 4.2.1.1) is essential for cells to acquire carbon and to cope with the low CO<SUB>2</SUB> environment under high salt conditions. For the first time, the present study describes the existence of eight genes coding for different types of <I>D. salina</I> CAs: five alpha-type (DsCAs) and three gamma-type (DsgCAs). Beta-type CAs appear to be lacking in <I>D. salina</I>, as they could not be found. Under either high salt or limited CO<SUB>2</SUB> condition, the CAs from <I>D. salina</I> showed different expression patterns, with phylogenetically close CAs exhibiting similar gene expression patterns. For the biological characterization of DsCA2b, which is a newly identified α-type CA, the enzyme was successfully produced as a soluble protein by truncating the membrane spanning regions at both ends (trDsCA2b). It was demonstrated that this truncated trDsCA2b version of the CA enzyme was active. Purified trDsCA2b clearly showed increased CA activity at increased NaCl concentrations of up to 3.0M. Based on in silico analysis and our predicted 3D structure of DsCA2b, we propose that this enzyme is localized in the plasma membrane of cells and active on the extracellular side. Our results are in agreement with the hypothesis that the DsCAs are essential enzymes for carbon acquisition mechanism under salt stress and CO<SUB>2</SUB> stress in <I>D. salina</I>.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Eight novel carbonic anhydrases (DsCAs) were identified in <I>D. salina</I> CCAP 19/18. </LI> <LI> <I>DsCAs</I> were regulated differently under salt and CO<SUB>2</SUB> stresses. </LI> <LI> The salt enhanced activity of recombinant DsCA2b endorses salt tolerance of <I>D. salina</I>. </LI> <LI> DsCAs are predicted to play the key role in carbon acquisition in <I>D. salina</I>. </LI> </UL> </P>
정성윤(Sungyun Jung),백광렬(Kwangryul Baek) 전력전자학회 2005 전력전자학술대회 논문집 Vol.- No.-
차량 내에 장착되는 전장품의 기능과 성능의 중요성은 점점 중요해지고 있다. 이에 따라, 자동차 내의 멀티미디어 기기인 오디오, 내비게이터, 스피커 등을 네트워크로 연결하여 사용자 편의성을 증대하고 첨단화 하는 시도로써 MOST(media oriented systems transport) 네트워크가 제안 되었다. 네트워크 통합화의 추세에 따라, 멀티미디어 전용 네트워크인 MOST를 차량용 제어 네트워크인 CAN에 접속하여 그 성능을 평가한다.