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John H. Koo(具璋會),Liu Jingxian,Zhao Aping,Wu Baozhu,Kwon Oh-sun 비교민속학회 1993 비교민속학 Vol.10 No.-
In the present study, we re-exame the plural for mation in Manchu, and attempt to describe more precisely the conditions under which various plural morphemes are used, using data drawn from resources of written and spoken Manchu. In the past, the research on this subject has been rather superficial, lacking sufficient documental support, particularly phonological interpretation. We argue that the plural formation is closely related to the vowel harmony in Manchu and to other non-linguistic factors as in some other Tungus-Manchu languages(eㆍgㆍ, Solon). The study concludes that the plural in Manchu cannot be adequately accounted for by linguistic analysis alone. It suggests that some cultural factors in the traditional Manchu society play a significant role in for ming the variety of plural forms.
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.