Salicylic acid-mediated innate immunity in Arabidopsis is regulated by SIZ1 SUMO E3 ligase

Reversible modifications of target proteins by small ubiquitin-like modifier (SUMO) proteins are involved in many cellular processes in yeast and animals. Yet little is known about the function of sumoylation in plants. Here, we show that the SIZ1 gene, which encodes an Arabidopsis SUMO E3 ligase, regulates innate immunity. Mutant siz1 plants exhibit constitutive systemic-acquired resistance (SAR) characterized by elevated accumulation of salicylic acid (SA), increased expression of pathogenesis-related (PR) genes, and increased resistance to the bacterial pathogen Pseudomonas syringae pv. tomato (Pst) DC3000. Transfer of the NahG gene to siz1 plants results in reversal of these phenotypes back to wild-type. Analyses of the double mutants, npr1 siz1, pad4 siz1 and ndr1 siz1 revealed that SIZ1 controls SA signalling. SIZ1 interacts epistatically with PAD4 to regulate PR expression and disease resistance. Consistent with these observations, siz1 plants exhibited enhanced resistance to Pst DC3000 expressing avrRps4, a bacterial avirulence determinant that responds to the EDS1/PAD4-dependent TIR-NBS-type R gene. In contrast, siz1 plants were not resistant to Pst DC3000 expressing avrRpm1, a bacterial avirulence determinant that responds to the NDR1-dependent CC-NBS-type R gene. Jasmonic acid (JA)-induced PDF1.2 expression and susceptibility to Botrytis cinerea were unaltered in siz1 plants. Taken together, these results demonstrate that SIZ1 is required for SA and PAD4-mediated R gene signalling, which in turn confers innate immunity in Arabidopsis.     

Differences in the metabolic responses of root tips of wheat and rye to aluminium stress

The effects of aluminium (Al) ions on the metabolism of root apical meristems were examined in 4-day-old seedlings of two cereals which differed in their tolerance to Al: wheat cv. Grana (Al-sensitive) and rye cv. Dakowskie Nowe (Al tolerant). During a 24 h incubation period in nutrient solutions containing 0.15 mM and 1.0 mM of Al for wheat and rye, respectively, the activity of first two enzymes in the pentose phosphate pathway (G-6-PDH and 6-PGDH) decreased in the sensitive cultivar. In the tolerant cultivar activities of these enzymes increased initially, then decreased slightly, and were at control levels after 24 h. In the Al-sensitive wheat cultivar a 50% reduction in the activity of 6-phosphogluconate dehydrogenase was observed in the presence of Al. Changes in enzyme activity were accompanied by changes in levels of G-6-P- the initial substrate in the pentose phosphate pathway. When wheat was exposed for 16 h to a nutrient solution containing aluminium, a 90% reduction in G-6-P concentration was observed. In the Al-tolerant rye cultivar, an increase and subsequently a slight decrease in G-6-P concentration was detected, and after 16 h of Al-stress the concentration of this substrate was still higher than in control plants. This dramatic Al-induced decrease in G-6-P concentration in the Al-sensitive wheat cultivar was associated with a decrease in both the concentration of glucose in the root tips as well as the activity of hexokinase, an enzyme which is responsible for phosphorylation of glucose to G-6-P. However, in the Al-tolerant rye cultivar, the activity of this enzyme remained at the level of control plants during Al-treatment, and the decrease in the concentration of glucose occurred at a much slower rate than in wheat. These results suggest that aluminium ions change cellular metabolism of both wheat and rye root tips. In the Al-sensitive wheat cultivar, irreversible disturbances induced by low doses of Al in the nutrient solution appear very quickly, whereas in the Al-tolerant rye cultivar, cellular metabolism, even under severe stress conditions, is maintained for a long time at a level which allows for root elongation to continue.Abbreviations G-6-PDH glucose-6-phosphate dehydrogenase - 6-PGDH 6-phosphogluconate dehydrogenase - G-6-P glucose-6-phosphate - TEA triethanolamine     

Structural Insight into Binding of the ZZ Domain of HERC2 to Histone H3 and SUMO1

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Functional expression of PHO1 to the Golgi and trans-Golgi network and its role in export of inorganic phosphate

Arabidopsis thaliana PHO1 is primarily expressed in the root vascular cylinder and is involved in the transfer of inorganic phosphate (Pi) from roots to shoots. To analyze the role of PHO1 in transport of Pi, we have generated transgenic plants expressing PHO1 in ectopic A. thaliana tissues using an estradiol-inducible promoter. Leaves treated with estradiol showed strong PHO1 expression, leading to detectable accumulation of PHO1 protein. Estradiol-mediated induction of PHO1 in leaves from soil-grown plants, in leaves and roots of plants grown in liquid culture, or in leaf mesophyll protoplasts, was all accompanied by the specific release of Pi to the extracellular medium as early as 2-3 h after addition of estradiol. Net Pi export triggered by PHO1 induction was enhanced by high extracellular Pi and weakly inhibited by the proton-ionophore carbonyl cyanide m-chlorophenylhydrazone. Expression of a PHO1-GFP construct complementing the pho1 mutant revealed GFP expression in punctate structures in the pericycle cells but no fluorescence at the plasma membrane. When expressed in onion epidermal cells or in tobacco mesophyll cells, PHO1-GFP was associated with similar punctate structures that co-localized with the Golgi/trans-Golgi network and uncharacterized vesicles. However, PHO1-GFP could be partially relocated to the plasma membrane in leaves infiltrated with a high-phosphate solution. Together, these results show that PHO1 can trigger Pi export in ectopic plant cells, strongly indicating that PHO1 is itself a Pi exporter. Interestingly, PHO1-mediated Pi export was associated with its localization to the Golgi and trans-Golgi networks, revealing a role for these organelles in Pi transport.