Čeština
EnglishArabidopsis non-specific phospholipase C1: characterization and its involvement in response to heat stress
Krčková Z., Brouzdová J., Daněk M., Kocourková D., Rainteau D., Ruelland E., Valentová O., Pejchar P., Martinec J.
FRONTIERS IN PLANT SCIENCE 6: 928, 2015
Keywords: non-specific phospholipase C, heat stress, Arabidopsis thaliana, phospholipids, diacylglycerol
Abstract: The Arabidopsis non-specific phospholipase C1 (NPC) protein family is encoded by the genes NPC1 – NPC6. It has been shown that NPC4 and NPC5 possess phospholipase C activity; NPC3 has lysophosphatidic acid phosphatase activity. NPC3, 4 and 5 play roles in the responses to hormones and abiotic stresses. NPC1, 2 and 6 has not been studied functionally yet. We found that Arabidopsis NPC1 expressed in Escherichia coli possesses phospholipase C activity in vitro. This protein was able to hydrolyse phosphatidylcholine to diacylglycerol. NPC1-green fluorescent protein was localized to secretory pathway compartments in Arabidopsis roots. In the knock out T-DNA insertion line NPC1 (npc1) basal thermotolerance was impaired compared with wild-type (WT); npc1 exhibited significant decreases in survival rate and chlorophyll content at the seventh day after heat stress (HS). Conversely, plants overexpressing NPC1 (NPC1-OE) were more resistant to HS compared with WT. These findings suggest that NPC1 is involved in the plant response to heat.
DOI: IEB authors: Jitka Brouzdová, Michal Daněk, Daniela Kocourková, Zuzana Krčková, Jan Martinec, Přemysl Pejchar
FRONTIERS IN PLANT SCIENCE 6: 928, 2015
Keywords: non-specific phospholipase C, heat stress, Arabidopsis thaliana, phospholipids, diacylglycerol
Abstract: The Arabidopsis non-specific phospholipase C1 (NPC) protein family is encoded by the genes NPC1 – NPC6. It has been shown that NPC4 and NPC5 possess phospholipase C activity; NPC3 has lysophosphatidic acid phosphatase activity. NPC3, 4 and 5 play roles in the responses to hormones and abiotic stresses. NPC1, 2 and 6 has not been studied functionally yet. We found that Arabidopsis NPC1 expressed in Escherichia coli possesses phospholipase C activity in vitro. This protein was able to hydrolyse phosphatidylcholine to diacylglycerol. NPC1-green fluorescent protein was localized to secretory pathway compartments in Arabidopsis roots. In the knock out T-DNA insertion line NPC1 (npc1) basal thermotolerance was impaired compared with wild-type (WT); npc1 exhibited significant decreases in survival rate and chlorophyll content at the seventh day after heat stress (HS). Conversely, plants overexpressing NPC1 (NPC1-OE) were more resistant to HS compared with WT. These findings suggest that NPC1 is involved in the plant response to heat.
DOI: IEB authors: Jitka Brouzdová, Michal Daněk, Daniela Kocourková, Zuzana Krčková, Jan Martinec, Přemysl Pejchar