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PMID:9032475
| Citation |
Linassier, C, MacDougall, LK, Domin, J and Waterfield, MD (1997) Molecular cloning and biochemical characterization of a Drosophila phosphatidylinositol-specific phosphoinositide 3-kinase. Biochem. J. 321 ( Pt 3):849-56 |
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| Abstract |
Molecular, biochemical and genetic characterization of phosphoinositide 3-kinases (PI3Ks) have identified distinct classes of enzymes involved in processes mediated by activation of cell-surface receptors and in constitutive intracellular protein trafficking events. The latter process appears to involve a PtdIns-specific PI3K first described in yeast as a mutant, vps34, defective in the sorting of newly synthesized proteins from the Golgi to the vacuole. We have identified a representative member of each class of PI3Ks in Drosophila using a PCR-based approach. In the present paper we describe the molecular cloning of a PI3K from Drosophila, P13K_59F, that shows sequence similarity to Vps34. PI3K_59F encodes a protein of 108 kDa co-linear with Vps34 homologues, and with three regions of sequence similarity to other PI3Ks. Biochemical characterization of the enzyme, by expression of the complete coding sequence as a glutathione S-transferase fusion protein in Sf9 cells, demonstrates that PI3K_59F is a PtdIns-specific PI3K that can utilize either Mg2+ or Mn2+. This activity is sensitive to inhibition both by non-ionic detergent (Nonidet P40) and by wortmannin (IC50 10 nM). PI3K_59F, therefore, conserves both the structural and biochemical properties of the Vps34 class of enzymes. |
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| Keywords |
Amino Acid Sequence; Androstadienes/pharmacology; Animals; Base Sequence; Chromatography, High Pressure Liquid; Chromatography, Thin Layer; Cloning, Molecular; DNA Primers; Drosophila; Lipids/analysis; Molecular Sequence Data; Phosphatidylinositol 3-Kinases; Phosphatidylinositols/metabolism; Phosphotransferases (Alcohol Group Acceptor)/chemistry; Recombinant Fusion Proteins/genetics; Sequence Analysis; Substrate Specificity |
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Significance
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