@Article{IPB-699, author = {Sharma, V.K. and Monostori, T. and Hause, B. and Maucher, H. and Göbel, C. and Hornung, E. and Hänsch, R. and Bittner, F. and Wasternack, C. and Feussner, I. and Mendel, R.R. and Schulze, J.}, title = {{Genetic transformation of barley to modify expression of a 13-lipoxygenase}}, year = {2005}, pages = {33-34 }, journal = {Acta Biol. Szeged }, url = {http://www2.sci.u-szeged.hu/ABS/2005/Acta%20HP/4933.pdf}, volume = {49}, abstract = {Immature scutella of barley were transformed with cDNA coding for a 13-li-poxygenase of barley (LOX-100) via particle bombardment. Regenerated plants were tested by PAT-assay, Western-analysis and PCR-screening. Immunocytochemical assay of T0 plants showed expression of the LOX cDNA both in the chloroplasts and in the cytosol, depending on the presence of the chloroplast signal peptide sequences in the cDNA. A few transgenic plants containing higher amounts of LOX-derived products have been found. These are the candidates for further analysis concerning pathogen resistance.} } @Article{IPB-856, author = {Quint, M. and Ito, H. and Zhang, W. and Gray, W.M.}, title = {{Characterization of a novel temperature-sensitive allele of the CUL1/AXR6 subunit of SCF ubiquitin-ligases}}, year = {2005}, pages = {371-383}, journal = {Plant J}, url = {http://onlinelibrary.wiley.com/doi/10.1111/j.1365-313X.2005.02449.x/full}, volume = {43}, abstract = { Selective protein degradation by the ubiquitin-proteasome pathway has emerged as a key regulatory mechanism in a wide variety of cellular processes. The selective components of this pathway are the E3 ubiquitin-ligases which act downstream of the ubiquitin-activating and -conjugating enzymes to identify specific substrates for ubiquitinylation. SCF-type ubiquitin-ligases are the most abundant class of E3 enzymes in Arabidopsis. In a genetic screen for enhancers of the tir1-1 auxin response defect, we identified eta1/axr6-3, a recessive and temperature-sensitive mutation in the CUL1 core component of the SCFTIR1 complex. The axr6-3 mutation interferes with Skp1 binding, thus preventing SCF complex assembly. axr6-3 displays a pleiotropic phenotype with defects in numerous SCF-regulated pathways including auxin signaling, jasmonate signaling, flower development, and photomorphogenesis. We used axr6-3 as a tool for identifying pathways likely to be regulated by SCF-mediated proteolysis and propose new roles for SCF regulation of the far-red light/phyA and sugar signaling pathways. The recessive inheritance and the temperature-sensitive nature of the pleiotropically acting axr6-3 mutation opens promising possibilities for the identification and investigation of SCF-regulated pathways in Arabidopsis.} }