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Cloning and direct G-protein regulation of phospholipase D from tobacco


Cloning and direct G-protein regulation of phospholipase D from tobacco



Biochimica et Biophysica Acta 1530(2-3): 172-183



ISSN/ISBN: 0006-3002

PMID: 11239820

DOI: 10.1016/s1388-1981(00)00182-7

Phospholipase D (PLD) and heterotrimeric G-proteins are involved in plant signal transduction pathways at the plasma membrane. There is evidence suggesting that PLD acts downstream from G-proteins, but a direct interaction of specific members has not been shown. In the present paper, a PLD cDNA clone was isolated from tobacco, expressed as a GST fusion in bacteria, and the recombinant protein was purified by glutathione affinity. Its enzymatic properties identified it as an alpha-type PLD. The alpha-subunit of a G-protein from tobacco was isolated in a similar way. Both proteins were functional in biochemical assays. When the G-protein was included in the PLD assay, a strong dosage-dependent inhibition of the PLD activity was observed. Different control proteins did not exhibit this inhibitory effect. When GST-NtGPalpha1 was activated by incubation with GTPgammaS the inhibitory activity was greatly reduced. These results provide a first indication for a direct regulation of PLDalpha by a heterotrimeric G-protein alpha-subunit in plants.

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Accession: 003681320

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