Abstract
We report the molecular cloning and sequence of a phosphoinositide-specific phopspholipase C (PI-PLC), an enzyme that is of particular interest because of its central role in cell signal transduction. The signals in question are those delivered by hormones to their cell-surface receptors that activate PI-PLC by means of a guanine nucleotide binding protein. Activation of the enzyme leads to the hydrolysis of phosphatidylinositol 4,5-bisphosphate to two second messengers, 1,2-diacylglycerol and inositol 1,4,5-trisphos-phate, the second of which ultimately mobilizes internal pools of calcium1,2. There are at least five PI-PLC isoenzymes, whose differences in structure and function are unknown3–10. We have focused on isoenzyme I, which we have recently purified and characterized from guinea pig uterus8. We have now determined the sequence of a full length complementary DNA of this isoenzyme from the rat. Although the sequence has little similarity with the only other sequenced PI-PLC isoenzyme11, it has a surprising degree of similarity to thioredoxins, protein co-factors in thiol-dependent redox reactions12.
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Bennett, C., Balcarek, J., Varrichio, A. et al. Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C. Nature 334, 268–270 (1988). https://doi.org/10.1038/334268a0
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DOI: https://doi.org/10.1038/334268a0
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