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Pn-AMP1, a Plant Defense Protein, Induces Actin Depolarization in Yeasts
Koo, Ja Choon,Lee, Boyoung,Young, Michael E.,Koo, Sung Chul,Cooper, John A.,Baek, Dongwon,Lim, Chae Oh,Lee, Sang Yeol,Yun, Dae-Jin,Cho, Moo Je Oxford University Press 2004 Plant & cell physiology Vol.45 No.11
<P>Pn-AMP1, <I>Pharbitis nil</I> antimicrobial peptide 1, is a small cysteine-rich peptide implicated in host-plant defense. We show here that Pn-AMP1 causes depolarization of the actin cytoskeleton in <I>Saccharomyces cerevisiae</I> and <I>Candida albicans</I>. Pn-AMP1 induces rapid depolarization of actin cables and patches within 15 min. Increased osmolarity or temperature induces transient actin depolarization and results in increased sensitivity to Pn-AMP1, while cells conditioned to these stresses show less sensitivity. Mutations in components of a cell wall integrity pathway (Wsc1p, Rom2p, Bck1p and Mpk1p), which regulate actin repolarization, result in increased sensitivity to Pn-AMP1. A genetic screen reveals that mutations in components of the α-1,6-mannosyltransferase complex (Mnn10p, Mnn11p and Och1p), which regulate mannosylation of cell wall proteins, confer resistance to Pn-AMP1. FITC-conjugated Pn-AMP1 localizes to the outer surface of the cell with no significant staining observed in spheroplasts. Taken together, these results indicate that cell wall proteins are determinants of resistance to Pn-AMP1, and the ability of a plant defense protein to induce actin depolarization is important for its antifungal activity.</P>
Pn-AMP1, a Plant Defense Protein, Induces Actin Depolarization in Yeasts
Koo, Ja-Choon,Lee, Boyoung,Michael E. Young,Koo, Sung-Chul,John A. Cooper,Baek, Dong-won,Lim, Chae-Oh,Lee, Sang-Yeol,Yun, Dae-Jin,Cho, Moo-Je Plant molecular biology and biotechnology research 2004 Plant molecular biology and biotechnology research Vol.2004 No.-
Pn-AMP1, Pharbitis nil antimicrobial peptide 1, is a small cysteine-rich peptide implicated in host-plant defense. We show here that Pn-AMP1 causes depolarization of the actin cytoskeleton in Saccharomyces cerevisiae and Candida albicans. Pn-AMP1 induces rapid depolarization of actin cables and patches within 15 min. Increased osmolarity or temperature induces transient actin depolarization and results in increased sensitivity to Pn-AMP1, while cells conditioned to these stresses show less sensitivity. Mutations in components of a cell wall integrity pathway (Wsc1p, Rom2p, Bck1p and Mpk1p), which regulate actin repolarization, result in increased sensitivity to Pn-AMP1. A genetic screen reveals that mutations in components of the α-1,6-mannosyltransferase complex (Mnn10p, Mnn11p and Och1p), which regulate mannosylation of cell wall proteins, confer resistance to Pn-AMP1. FITC-conjugated Pn-AMP1 localizes to the outer surface of the cell with no significant staining observed in spheroplasts. Taken together, these results indicate that cell wall proteins are determinants of resistance to Pn-AMP1, and the ability of a plant defense protein to induce actin depolarization is important for its antifungal activity.
High-frequency Plant Regeneration from Cultured Flower Bud Receptacles of Allium hookeri L.
Koo, Ja Choon Korean Society of Horticultural Science 2014 원예과학기술지 Vol.32 No.5
Allium hookeri L. (Alliaceae family) is an important ethnomedicinal plant native to the Himalayan region of Asia. The aim of this research was to establish a high-frequency plant regeneration system for in vitro propagation of A. hookeri. Among the tissue types examined, receptacle explants derived from immature flower buds showed the highest regeneration rate of shoots ($93.33{\pm}4.63%$), roots ($76.67{\pm}7.85%$), and calli ($80.00{\pm}7.43%$) when cultured on Gamborg B5 (B5) medium containing $10{\mu}M$ 6-benzylaminopurine (BA) + $1{\mu}M$ naphthalene acetic acid (NAA), $0.5{\mu}M$ BA + $5{\mu}M$ NAA, and $1{\mu}M$ BA + $10{\mu}M$ NAA, respectively. Shoot multiplication was superior when cultured in liquid rather than on solid medium and relatively high concentrations of BA, ranging from 5 to $10{\mu}M$. Efficient bulblet formation following root induction from shoot clumps was achieved with culture in liquid B5 medium containing 7% (w/v) sucrose. Regenerated bulblets were successfully acclimatized to ex vitro conditions with a greater than 95% survival rate. By this method, a maximum of 62 plantlets per receptacle could be propagated within 9 weeks of initial culture. The in vitro propagation system established in this study will promote A. hookeri biotechnology, including large-scale production of healthy and aseptic clones, preserving parental genotypes with desirable traits, and genetic manipulation to enhance medicinal value.
Isolation of an actin promoter for strong expression of transgenes in the orchid genus Dendrobium
Koo, Ja Choon The Korean Society of Plant Biotechnology 2013 식물생명공학회지 Vol.40 No.1
We isolated and functionally characterized a Dendrobium Actin1 (DmACT1) promoter that drives strong gene expression in the orchid genus Dendrobium. A genomic fragment containing the region 3227 bp upstream of the coding region of DmACT1 was obtained by inverse PCR. Detailed comparison of the full-length cDNA and genomic sequences revealed that DmACT1 has a 1374 bp first intron in the 5' UTR. However, the 5' flanking sequences upstream of the coding region showed no obvious sequence similarities compared to those of known promoters, including plant actin promoters. Serial deletion constructs of the 5' flanking region from the translation initiation codon were fused to the coding sequence of a GUS/luciferase fusion reporter to identify the regulatory elements necessary for promoter activity. Transient assays in the flowers of Dendrobium revealed that the 5' UTR-intron greatly enhanced promoter activity. Moreover, the DmACT1 promoter with its 5' UTR-intron yielded approximately 10-fold higher reporter activity than the rice Act1 promoter-intron. Our data suggest that the DmACT1 promoter with its 5' UTR-intron is a useful tool for strong expression of transgenes in Dendrobium orchids.
( Ja Choon Koo ),( Yeo Chang Youn ),( Mi Sun Park ),( Myeong Eun Kim ) 한국임학회 2012 한국임학회 학술발표논문집 Vol.2012 No.-
South Korea is not included in Annex I countries under the Kyoto protocol. However, its greenhouse gas (GHG) emissions were listed 9th highest in the world. South Korean government announced a goal of reducing GHG emissions by 30 percent compared to the business as usual by 2020. In order to achieve this voluntary emission target effectively, public and private sector have tried to introduce appropriate mitigation methods in various sectors such as energy, transportation and so on. In particular, the forest sector can play a significant role in mitigating greenhouse gases through carbon sequestration because about 64% of total land is covered by forest in South Korea. In this background, Korea Forest Service has been preparing a policy instrument to make forest carbon credits be traded in the voluntary carbon market which will be launched in 2015 in South Korea. Before introduction of the carbon market, it is needed to analyze companies` demands and preferences to forest carbon credit in advance. This research aimed to estimate the willingness to pay (WTP) of private companies in South Korea for carbon credits from forest offset projects such as domestic forest management activities and REDD (reducing emissions from deforestation and forest degradation) in developing countries. We postulate null hypotheses that there is no difference in the WTP according to types of forest offset projects. The face to face interview was conducted with 200 companies engaged in various types of business in 2011. 70 valid responses were analyzed to elicit the value of WTP for carbon credits per ton of CO2 equivalent by non-parametric approach (Turnbull estimation). We found that there was a difference in WTP according to the area of forest offset project. Estimated WTPs for forest carbon credits were 4.55~7.86 USD/tCO2 in domestic project and 6.64~11.05 USD/tCO2 in foreign project. These results can contribute to designing forest carbon market considering primary consumers.
Koo, Ja-Choon,Chun, Hyun-Jin,Park, Hyeong-Cheol,Kim, Min-Chul,Koo, Yoon-Duck,Koo, Seong-Cheol,Ok, Hyun-Mi,Park, Soo-Jeong,Lee, Sung-Ho,Yun, Dae-Jin,Lim, Chae-Oh,Bahk, Jeong-Dong,Lee, Sang-Yeol,Cho, Mo Plant molecular biology and biotechnology research 2002 Plant molecular biology and biotechnology research Vol.2002 No.-
Two hevein-like peptides from the seed of Pharbitis nil, designated Pharbitis nil antimicrobial peptide 1 (Pn-AMP1) and Pn-AMP2, had been purified previously. Both exhibit potent in vitro antifungal activity against a broad spectrum of phytopathogenic fungi. We now report the isolation of two cDNA clones, designated pnAMP-h1 and pnAMP-h2, and the corresponding genomic clones encoding these protein suggests that the peptides are produced as a prepropeptide consisting of and N-terminal signal peptide, the mature protein and C-terminal domains. The transcripts of the two genes are accumulated seed-specifically, and the maximum transcripts are observed in the mid-to-late stage of seed development. Constitutive over-expression of the pnAMP-h2 cDNA in transgenic tobacco under the control of the cauliflower mosaic virus 35S promoter conferred enhanced resistance against the oomycete Phytophthora parasitica, the causal agent of black shank disease. Thus the Pn-AMPs may play a role in the protection of seeds and may