Contribution of isopentenyl phosphate to plant terpenoid metabolism

Nature Plants

Volumn 4, Issue 9, 2018, Pages 721-729

  Henry, Laura K ^a   Thomas, Suzanne T ^b   Widhalm, Joshua R ^a   Lynch, Joseph H ^a   Davis, Thomas C ^a   Kessler, Sharon A ^a   Bohlmann, Jörg ^c   Noel, Joseph P ^b,d   Dudareva, Natalia ^a  

^a PURDUE UNIVERSITY   (United States)

^b SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^c UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^d HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HEMITERPENE; ISOPENTENYL DIPHOSPHATE; ORGANOPHOSPHORUS COMPOUND; PHOSPHOTRANSFERASE; PLANT PROTEIN; TERPENE;

ARABIDOPSIS; METABOLISM; TOBACCO; TRANSGENIC PLANT;

ARABIDOPSIS; HEMITERPENES; METABOLIC NETWORKS AND PATHWAYS; ORGANOPHOSPHORUS COMPOUNDS; PHOSPHOTRANSFERASES; PLANT PROTEINS; PLANTS, GENETICALLY MODIFIED; TERPENES; TOBACCO;

EID: 85052551488     PISSN: None     EISSN: 20550278     Source Type: Journal    
DOI: 10.1038/s41477-018-0220-z     Document Type: Article

References (40)

1. Hemmerlin, A., Harwood, J. L. & Bach, T. J. A raison d’être for two distinct pathways in the early steps of plant isoprenoid biosynthesis? Prog. Lipid Res. 51, 95–148 (2012)
2. Tholl, D. Biosynthesis and biological functions of terpenoids in plants. Adv. Biochem. Eng. Biotechnol. 148, 63–106 (2015)
3. Gershenzon, J. & Dudareva, N. The function of terpene natural products in the natural world. Nat. Chem. Biol. 3, 408–414 (2007)
4. Tippmann, S., Chen, Y., Siewers, V. & Nielsen, J. From flavors and pharmaceuticals to advanced biofuels: Production of isoprenoids in Saccharomyces cerevisiae. Biotechnol. J. 8, 1435–1444 (2013)
5. Zerbe, P. & Bohlmann, J. Plant diterpene synthases: Exploring modularity and metabolic diversity for bioengineering. Trends Biotechnol. 33, 419–428 (2015)
6. Vranová, E., Coman, D. & Gruissem, W. Network analysis of the MVA and MEP pathways for isoprenoid synthesis. Annu. Rev. Plant Biol. 64, 665–700 (2013)
7. Hemmerlin, A. Post-translational events and modifications regulating plant enzymes involved in isoprenoid precursor biosynthesis. Plant Sci. 203–204, 41–54 (2013)
8. Vickers, C. E., Bongers, M., Liu, Q., Delatte, T. & Bouwmeester, H. Metabolic engineering of volatile isoprenoids in plants and microbes. Plant Cell Environ. 37, 1753–1775 (2014)
9. Wu, S. et al. Redirection of cytosolic or plastidic isoprenoid precursors elevates terpene production in plants. Nat. Biotechnol. 24, 1441–1447 (2006)
10. Farhi, M. et al. Generation of the potent anti-malarial drug artemisinin in tobacco. Nat. Biotechnol. 29, 1072–1074 (2011)
11. Muñoz-Bertomeu, J., Sales, E., Ros, R., Arrillaga, I. & Segura, J. Up-regulation of an N-terminal truncated 3-hydroxy-3-methylglutaryl CoA reductase enhances production of essential oils and sterols in transgenic Lavandula latifolia. Plant Biotechnol. J. 5, 746–758 (2007)
12. Liao, P., Hemmerlin, A., Bach, T. J. & Chye, M.-L. The potential of the mevalonate pathway for enhanced isoprenoid production. Biotechnol. Adv. 34, 697–713 (2016)
13. Dellas, N., Thomas, S. T., Manning, G. & Noel, J. P. Discovery of a metabolic alternative to the classical mevalonate pathway. eLife 2, e00672 (2013)
14. Henry, L. K., Gutensohn, M., Thomas, S. T., Noel, J. P. & Dudareva, N. Orthologs of the archaeal isopentenyl phosphate kinase regulate terpenoid production in plants. Proc. Natl Acad. Sci. USA 112, 10050–10055 (2015)
15. VanNice, J. C. et al. Identification in Haloferax volcanii of phosphomevalonate decarboxylase and isopentenyl phosphate kinase as catalysts of the terminal enzyme reactions in an archaeal alternate mevalonate pathway. J. Bacteriol. 196, 1055–1063 (2014)
16. Karačić, Z. et al. A novel plant enzyme with dual activity: an atypical Nudix hydrolase and a dipeptidyl peptidase III. Biol. Chem. 398, 101–112 (2017)
17. Kraszewska, E. The plant Nudix hydrolase family. Acta Biochim. Pol. 55, 663–671 (2008)
18. McLennan, A. G. Substrate ambiguity among the nudix hydrolases: biologically significant, evolutionary remnant, or both? Cell. Mol. Life Sci. 70, 373–385 (2013)
19. Ogawa, T. et al. Molecular characterization of organelle-type Nudix hydrolases in Arabidopsis. Plant Physiol. 148, 1412–1424 (2008)
20. Ogawa, T., Ueda, Y., Yoshimura, K. & Shigeoka, S. Comprehensive analysis of cytosolic nudix hydrolases in Arabidopsis thaliana. J. Biol. Chem. 280, 25277–25283 (2005)
21. Yoshimura, K., Ogawa, T., Ueda, Y. & Shigeoka, S. AtNUDX1, an 8-oxo-7,8-dihydro-2′-deoxyguanosine 5′-triphosphate pyrophosphohydrolase, is responsible for eliminating oxidized nucleotides in Arabidopsis. Plant Cell Physiol. 48, 1438–1449 (2007)
22. Liu, J. et al. Structural insights into the substrate recognition mechanism of Arabidopsis GPP-bound NUDX1 for noncanonical monoterpene biosynthesis. Molecular Plant 11, 218–221 (2018)
23. Svensson, L. M. et al. Crystal structure of human MTH1 and the 8-oxo-dGMP product complex. FEBS Lett. 585, 2617–2621 (2011)
24. Nakamura, T. et al. Structural and dynamic features of the MutT protein in the recognition of nucleotides with the mutagenic 8-oxoguanine base. J. Biol. Chem. 285, 444–452 (2010)
25. Magnard, J.-L. et al. Biosynthesis of monoterpene scent compounds in roses. Science 349, 81–83 (2015)
26. Jones, C. G. et al. Sandalwood fragrance biosynthesis involves sesquiterpene synthases of both the terpene synthase (TPS)-a and TPS-b subfamilies, including santalene synthases. J. Biol. Chem. 286, 17445–17454 (2011)
27. Simkin, A. J. et al. Peroxisomal localisation of the final steps of the mevalonic acid pathway in planta. Planta 234, 903–914 (2011)
28. Reumann, S., Chowdhary, G. & Lingner, T. Characterization, prediction and evolution of plant peroxisomal targeting signals type 1 (PTS1s). Biochim. Biophys. Acta Mol. Cell Res. 1863, 790–803 (2016)
29. Curtis, I. S., Davey, M. R. & Power, J. B. Leaf disk transformation. Methods Mol. Biol. 44, 59–70 (1995)
30. Sparkes, I. A., Runions, J., Kearns, A. & Hawes, C. Rapid, transient expression of fluorescent fusion proteins in tobacco plants and generation of stably transformed plants. Nat. Protoc. 1, 2019–2025 (2006)
31. Nelson, B. K., Cai, X. & Nebenführ, A. A multicolored set of in vivo organelle markers for co-localization studies in Arabidopsis and other plants. Plant J. 51, 1126–1136 (2007)
32. Yoo, H. et al. An alternative pathway contributes to phenylalanine biosynthesis in plants via a cytosolic tyrosine:phenylpyruvate aminotransferase. Nat. Commun. 4, 2833 (2013)
33. Powell, H. R., Battye, T. G. G., Kontogiannis, L., Johnson, O. & Leslie, A. G. W. Integrating macromolecular X-ray diffraction data with the graphical user interface iMosflm. Nat. Protoc. 12, 1310–1325 (2017)
34. Evans, P. R. & Murshudov, G. N. How good are my data and what is the resolution? Acta Crystallogr. D 69, 1204–1214 (2013)
35. Vagin, A. & Teplyakov, A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022–1025 (1997)
36. Stein, N. et al. CHAINSAW: a program for mutating pdb files used as templates in molecular replacement. J. Appl. Crystallogr. 41, 641–643 (2008)
37. Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126–2132 (2004)
38. Terwilliger, T. C. et al. Iterative model building, structure refinement and density modification with the PHENIX AutoBuildwizard. Acta Crystallogr. D 64, 61–69 (2008)
39. Curtis, M. D. & Grossniklaus, U. A Gateway cloning vector set for high-throughput functional analysis of genes in plants. Breakthr. Technol. 133, 462–469 (2003)
40. Clough, S. J. & Bent, A. F. Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16, 735–743 (1998)