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Arabidopsis non-specific phospholipase C1: characterization and its involvement in response to heat stress.


ABSTRACT: The Arabidopsis non-specific phospholipase C (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.

SUBMITTER: Krckova Z 

PROVIDER: S-EPMC4631941 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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Arabidopsis non-specific phospholipase C1: characterization and its involvement in response to heat stress.

Krčková Zuzana Z   Brouzdová Jitka J   Daněk Michal M   Kocourková Daniela D   Rainteau Dominique D   Ruelland Eric E   Valentová Olga O   Pejchar Přemysl P   Martinec Jan J  

Frontiers in plant science 20151104


The Arabidopsis non-specific phospholipase C (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 pho  ...[more]

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