Involvement of phospholipase A2 in the response of Solanum species to an elicitor from Phytophtora infestans

• Autorzy: Polkowska-Kowalczyk L. , Wielgat B. , Maciejewska U.
• Języki publikacji: EN

Abstrakty

EN

Changes in activity of phospholipase A₂ (PLA₂), a key enzyme in lipid metabolism and signal network in defence mechanisms, were investigated in Solanum species and Phytophthora infestans interaction. We have compared PLA₂ activity in response to an elicitor, a culture filtrate (CF) derived from P. infestans, in non-host resistant Solanum nigrum var. gigantea, field resistant S. tuberosum cv Bzura and susceptible S. tuberosum clone H-8105. To elucidate the contribution of specific forms of PLA₂ to plant defence mechanism reasonably selective PLA₂ inhibitors, haloenol lactone suicide substrate (HELSS) and p-bromophenacyl bromide (BPB), which discriminate between Ca⁺²-independent PLA₂ (iPLA₂) and Ca⁺²-dependent secretory PLA₂ (sPLA₂), were used. The in vivo and in vitro effects of the inhibitors on PLA₂ activity and on generation of reactive oxygen species (ROS) induced by CF in the studied plants were assayed. We found that PLA₂ activity increased in response to CF treatment, displaying various kinetics and intensity depending on the resistance status of a given genotype. Differences among the genotypes in the effects of each inhibitor on CF-induced PLA₂ activity and on ROS production may reflect the diversity of PLA₂ isoforms in plants. Contrary to BPB, the inhibitory effect of HELSS was observable mainly on CF-induced PLA₂ activity, which suggests that iPLA₂ participates in signal transduction in defence reactions. Various effects of the two inhibitors on PLA₂ activity and ROS production suggest different contribution of sPLA₂ and iPLA₂ to modulation of defence reactions in the interaction between Solanum genotypes and P. infestans.

• Wydawca: -
• Czasopismo: Acta Physiologiae Plantarum
• Rocznik: 2011
• Tom: 33
• Numer: 6
• Opis fizyczny: p.2521-2531,fig.,ref.

Twórcy

autor

Polkowska-Kowalczyk L.

• Department of Plant Biochemistry, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warsaw, Poland

autor

Wielgat B.

• Department of Plant Biochemistry, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warsaw, Poland

autor

Maciejewska U.

• Department of Plant Biochemistry, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warsaw, Poland

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