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Original Articles

Cloning, Expression, and Characterization of a Thermostable PAP2L2, a New Member of the Type-2 Phosphatidic Acid Phosphatase Family from Geobacillus toebii T-85

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Pages 3134-3141 | Received 02 May 2008, Accepted 08 Sep 2008, Published online: 22 May 2014

  • 1) Stukey, J., and Carman, G. M., Identification of a novel phosphatase sequence motif. Protein Sci., 6, 469–472 (1997).
  • 2) Waggoner, D. W., Gomez-Munoz, A., Dewald, J., and Brindley, D. N., Phosphatidate phosphohydrolase catalyzes the hydrolysis of ceramide 1-phosphate, lysophosphatidate, and sphingosine 1-phosphate. J. Biol. Chem., 271, 16506–16509 (1996).
  • 3) Sigal, Y. J., McDermott, M. I., and Morris, A. J., Integral membrane lipid phosphatases/phosphotransferases: common structure and diverse functions. Biochem. J., 387, 281–293 (2005).
  • 4) Brindley, D. N., English, D., Pilquil, C., Buri, K., and Ling, Z. C., Lipid phosphate phosphatases regulate signal transduction through glycerolipids and sphingolipids. Biochim. Biophys. Acta, 1582, 33–44 (2002).
  • 5) Sciorra, V. A., and Morris, A. J., Roles for lipid phosphate phosphatases in regulation of cellular signaling. Biochim. Biophys. Acta, 1582, 45–51 (2002).
  • 6) Carman, G. M., and Han, G. S., Roles of phosphatidate phosphatase enzymes in lipid metabolism. Trends Biochem. Sci., 31, 694–699 (2006).
  • 7) Zhang, N., Zhang, J., Purcell, K. J., Cheng, Y., and Howard, K., The Drosophila protein wunen repels migrating germ cells. Nature, 385, 64–67 (1997).
  • 8) Barila, D., Plateroti, M., Nobili, F., Muda, A. O., Xie, Y., Morimoto, T., and Perozzi, G., The Dri42 gene, whose expression is up-regulated during epithelial differentiation, encodes a novel endoplasmic reticulum resident transmembrane protein. J. Biol. Chem., 271, 29928–29936 (1996).
  • 9) Hooksa, S. B., Raganb, S. P., and Lyncha, K. R., Identification of a novel human phosphatidic acid phosphatase type 2 isoform. FEBS Lett., 427, 188–192 (1998).
  • 10) Sun, L. Y., Gu, S. H., Sun, Y. Q., Zheng, D., Wu, Q. H., Li, X., Dai, J. F., Dai, J. L., Ji, C. N., Xie, Y., and Mao, Y. M., Cloning and characterization of a novel human phosphatidic acid phosphatase type 2, PAP2d, with two different transcripts PAP2d v1 and PAP2d v2. Mol. Cell Biochem., 272, 91–96 (2005).
  • 11) Bernard, R., Ghachi, M. E., Mengin-Lecreulx, D., Chippaux, M., and Denizot, F., BcrC from Bacillus subtilis acts as an undecaprenyl pyrophosphate phosphatase in bacitracin resistance. J. Biol. Chem., 280, 28852–28857 (2005).
  • 12) Ghachi, M. E., Derbise, A., Bouhss, A., and Mengin-Lecreulx, D., Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli. J. Biol. Chem., 280, 18689–18695 (2005).
  • 13) Neuwald, A. F., An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases. Protein Sci., 6, 1764–1767 (1997).
  • 14) Ishikawa, K., Mihara, Y., Gondoh, K., Suzuki, E., and Asano, Y., X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate. EMBO J., 19, 2412–2423 (2000).
  • 15) Toke, D. A., McClintick, M. L., and Carman, G. M., Mutagenesis of the phosphatase sequence motif in diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae. Biochemistry, 38, 14606–14613 (1999).
  • 16) Zhang, Q. X., Pilquil, C. S., Dewald, J., Berthiaume, L. G., and Brindley, D. N., Identification of structurally important domains of lipid phosphate phosphatase-1: implications for its sites of action. Biochem. J., 280, 181–184 (2005).
  • 17) Adams, M. W., and Kelly, R. M., Finding and using hyperthermophilic enzymes. Trends Biotechnol., 16, 329–332 (1998).
  • 18) Sambrook, J., and Russell, D. W., “Molecular Cloning, a Laboratory Manual” 3rd edn., Cold Spring Harbor Press, Cold Spring Harbor (2001).
  • 19) Takeuchi, M., Harigai, M., Momohara, S., Ball, E., Abe, J., Furuichi, K., and Kamatani, N., Cloning and characterization of DPPL1 and DPPL2, representatives of a novel type of mammalian phosphatidate phosphatase. Gene, 399, 174–180 (2007).
  • 20) Carman, G. M., Deems, R. A., and Dennis, E. A., Lipid signaling enzymes and surface dilution kinetics. J. Biol. Chem., 270, 18711–18714 (1995).
  • 21) Marchesi, J. R., Sato, T., Weightman, A. J., Martin, T. A., Fry, J. C., Hiom, S. J., Dymock, D., and Wade, W. G., Design and evaluation of useful bacterium-specific PCR primers that amplify genes coding for bacterial 16S rRNA. Appl. Environ. Microbiol., 64, 795–799 (1998).
  • 22) Kyte, J., and Doolittle, R. F., A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 157, 105–132 (1982).
  • 23) Kashino, Y., Separation methods in the analysis of protein membrane complexes. J. Chromatogr. B, 797, 191–216 (2003).
  • 24) Gasteiger, E., Gattiker, A., Hoogland, C., Ivany, I., Appel, R. D., and Bairoch, A., ExPasy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res., 31, 3784–3788 (2003).
  • 25) Roberts, R., Sciorra, V. A., and Morris, A. J., Human type 2 phosphatidic acid phosphohydrolases substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J. Biol. Chem., 273, 22059–22067 (1998).
  • 26) Dillon, D. A., Wu, W. I., Riedel, B., Wissing, J. B., Dowhan, W., and Carman, G. M., The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity. J. Biol. Chem., 271, 30548–30553 (1996).
  • 27) Wu, W. I., Liu, Y., Riedel, B., Wissing, J. B., Fischl, A. S., and Carman, G. M., Purification and characterization of diacylglycerol pyrophosphate phosphatase from Saccharomyces cerevisiae. J. Biol. Chem., 271, 1868–1876 (1996).
  • 28) Fleming, I. N., and Yeaman, S. J., Purification and characterization of N-ethylmaleimide-insensitive phosphatidic acid phosphohydrolase (PAP2) from rat liver. Biochem. J., 308, 983–989 (1995).

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