Abstract. The cut hypocotyl of Ricinus communis L.seedlings exudes phloem sap which contains a characteristic set of proteins (Sakuth et al. 1993, Planta 191, 207-213). These sieve-tube exudate proteins were probed with antibodies to highly conserved proteins, namely ribulose-1,5-bisphosphate carboxylase-oxygenase (Rubisco), Rubisco-subunit-binding protein, heat-shock protein (HSP 70), chaperonin GroEL and ubiquitin. Homologous proteins in the sieve-tube exudate were identified with antisera to HSP 70, Rubisco-subunit-binding protein and ubiquitin. Ribulose-l,5-bisphosphate carboxylase-oxygenase, which was present in the tissue, was not detected. Of all the cross-reactive proteins detected, ubiquitin was special because the ubiquitin-to-protein ratio in the sieve-tube exudate was higher than in both the surrounding hypocotyl and in the cotyledonary tissues. Therefore, ubiquitin features properties which favour its transfer into the sieve tubes and which might rely on efficient transport through plasmodesmata. It is assumed that chaperones and ubiquitin are needed for the maintenance of sieve-tube function, e.g. to ensure correct folding of proteins. Their possible involvement in protein translocation through plasmodesmata from companion cells to sieve tubes is discussed.
Abstract. Ricinus communis L. seedlings exuded pure phloem sap from the cut hypocotyl for several hours. Throughout the entire exudation period proteins were present in the phloem exudate at a constant concentration ranging from 0.11 to 0.41 mg. ml 1 depending on the culture conditions and the age of the seedlings. Manipulation of the nutrient supply at the cotyledons after removal of the endosperm did not change the protein concentration in the exudate. Comparison of sieve-tube exudate proteins (STEPs) with soluble proteins extracted from the hypocotyl and the cotyledons showed a unique abundance of small proteins in the exudate, with molecular weights ranging from 10 to 25 kDa. Bands at 18, 19 and 20kDa were especially dominant. The proteins found transiently in the xylem exudate, which might represent proteins secreted at the wound surface, were different in pattern. Two-dimensional separation of STEPs revealed that more than 100 distinct polypeptides occurred in the sieve-tube exudate, most of them slightly acidic with isoelectric points ranging from 4 to 6 and a few basic ones around 8.[35S]Methionine fed to the cotyledons led to labelling of STEPs, demonstrating their rapid synthesis. It is concluded that there is a continuous synthesis and translocation of specific sieve-tube proteins, whose function is unknown.
We compared the enzymatic antioxidative defence mechanisms of some regional subspecies of Allium (A. cepa L., A. ascalonicum auct. hort., A. sativum L.) cultivated mainly in the western regions of Romania, and two modern Hungarian climate resistant F 1 hybrids. The variability in the activities of antioxidant enzymes superoxide dismutase (SOD), catalase (CAT), peroxidase (POD), glutathione reductase (GR) and glutathione S-transferase (GST) and their changes under soil moisture stress were investigated. 1-week-long water stress revealed that among three Allium species, relative water content decreased only in A. ascalonicum leaves (up to 16%). Unlike root enzymes, the activities of the shoot enzymes, especially POD, GR and GST showed a stronger correlation with the water content of the leaves after one week of water withdrawal; regression coefficients (R 2 ) were 0.359, 0.518 and 0.279, respectively. The ancient populations with elevated (or highly inducible) antioxidant enzyme activities may be interesting for further research and for breeding of new Allium varieties.
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