A gene encoding a phosphatidylinositol-specific phospholipase C is induced by dehydration and salt stress in Arabidopsis thaliana

Takashi Hirayama, C. Ohto, T. Mizoguchi, K. Shinozaki

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277 Citations (Scopus)

Abstract

A cDNA corresponding to a putative phosphatidylinositol-specific phospholipase C (PI-PLC) in the higher plant Arabidopsis thaliana was cloned by use of the polymerase chain reaction. The cDNA, designated cAtPLC1, encodes a putative polypeptide of 561 aa with a calculated molecular mass of 54 RDa. The putative product includes so-called X and Y domains found in all PI-PLCs identified to date. In mammalian cells, there are three types of PI- PLC, PLC-β, -γ, and -δ. The overall structure of the putative AtPLC1 protein is most similar to that of PLC-δ, although the AtPLC1 protein is much smaller than PLCs from other organisms. The recombinant AtPLC1 protein synthesized in Escherichia coli was able to hydrolyze phosphatidylinositol 4,5-bisphosphate and this activity was completely dependent on Ca2+, as observed also for mammalian PI-PLCs. These results suggest that the AtPLC1 gene encodes a genuine PI-PLC of a higher plant. Northern blot analysis showed that the AtPLC1 gene is expressed at very low levels in the plant under normal conditions but is induced to a significant extent under various environmental stresses, such as dehydration, salinity, and low temperature. These observations suggest that AtPLC1 might be involved in the signal- transduction pathways of environmental stresses and that an increase in the level of AtPLC1 might amplify the signal, in a manner that contributes to the adaptation of the plant to these stresses.

Original languageEnglish
Pages (from-to)3903-3907
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number9
Publication statusPublished - 1995
Externally publishedYes

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Phosphoinositide Phospholipase C
Dehydration
Arabidopsis
Salts
Genes
Complementary DNA
Salinity
Phosphatidylinositols
Recombinant Proteins
Northern Blotting
Signal Transduction
Proteins
Escherichia coli
Polymerase Chain Reaction
Peptides
Temperature

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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abstract = "A cDNA corresponding to a putative phosphatidylinositol-specific phospholipase C (PI-PLC) in the higher plant Arabidopsis thaliana was cloned by use of the polymerase chain reaction. The cDNA, designated cAtPLC1, encodes a putative polypeptide of 561 aa with a calculated molecular mass of 54 RDa. The putative product includes so-called X and Y domains found in all PI-PLCs identified to date. In mammalian cells, there are three types of PI- PLC, PLC-β, -γ, and -δ. The overall structure of the putative AtPLC1 protein is most similar to that of PLC-δ, although the AtPLC1 protein is much smaller than PLCs from other organisms. The recombinant AtPLC1 protein synthesized in Escherichia coli was able to hydrolyze phosphatidylinositol 4,5-bisphosphate and this activity was completely dependent on Ca2+, as observed also for mammalian PI-PLCs. These results suggest that the AtPLC1 gene encodes a genuine PI-PLC of a higher plant. Northern blot analysis showed that the AtPLC1 gene is expressed at very low levels in the plant under normal conditions but is induced to a significant extent under various environmental stresses, such as dehydration, salinity, and low temperature. These observations suggest that AtPLC1 might be involved in the signal- transduction pathways of environmental stresses and that an increase in the level of AtPLC1 might amplify the signal, in a manner that contributes to the adaptation of the plant to these stresses.",
author = "Takashi Hirayama and C. Ohto and T. Mizoguchi and K. Shinozaki",
year = "1995",
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T1 - A gene encoding a phosphatidylinositol-specific phospholipase C is induced by dehydration and salt stress in Arabidopsis thaliana

AU - Hirayama, Takashi

AU - Ohto, C.

AU - Mizoguchi, T.

AU - Shinozaki, K.

PY - 1995

Y1 - 1995

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