نتایج جستجو برای: in planta
تعداد نتایج: 16978227 فیلتر نتایج به سال:
HopQ1 (for Hrp outer protein Q), a type III effector secreted by Pseudomonas syringae pv phaseolicola, is widely conserved among diverse genera of plant bacteria. It promotes the development of halo blight in common bean (Phaseolus vulgaris). However, when this same effector is injected into Nicotiana benthamiana cells, it is recognized by the immune system and prevents infection. Although the ...
The ability to move DNA into an organism and thereby alter its phenotype is central to both basic and applied molecular biology. Transformation is a simple task with Escherichia coli or Saccharomyces cerevisiae, but is usually more difficult with multicellular eukaryotes and can be particularly challenging with some important plant species. However, for Arabidopsis, in planta transformation met...
We report here the in planta production of the recombinant vaccinia virus B5 antigenic domain (pB5), an attractive component of a subunit vaccine against smallpox. The antigenic domain was expressed by using efficient transient and constitutive plant expression systems and tested by various immunization routes in two animal models. Whereas oral administration in mice or the minipig with collard...
Metabolism of the alpha-1,1 glucose disaccharide, trehalose, is indispensable in plants. In the Murashigeand Skoog (MS) medium, trehalose inhibits plant growth and allocation of carbon to roots. A suppressorof trehalose-6-phosphate (T6P) mediated growth arrest, GR-RBP2, is characterized in more detail.Phylogenetic analysis revealed that GR-RBP2 is a protein of likely prokaryot...
The NADPH-dependent protochlorophyllide (Pchlide) oxidoreductase (POR) is unique because it is a photoenzyme that requires light for its catalytic activity and uses Pchlide itself as a photoreceptor. In Arabidopsis, there are three structurally related PORs, denoted PORA, PORB, and PORC. The import of one of them, PORA, into plastids of cotyledons is substrate dependent. This substrate dependen...
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