A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases

Biochemical Journal

Volumn 439, Issue 3, 2011, Pages 375-379

  Kleczkowski, Leszek A ^a   Geisler, Matt ^b   Fitzek, Elisabeth ^b   Wilczynska, Malgorzata ^a  

^a UMEÅ UNIVERSITY   (Sweden)

^b SOUTHERN ILLINOIS UNIVERSITY   (United States)

Author keywords

Oligomerization; Protein structure; Sugar activation; UDP sugar synthesis

Indexed keywords

TRANSFER RNA; URIDINE DIPHOSPHATE SUGAR; URIDINE TRIPHOSPHATE GLUCOSE 1 PHOSPHATE URIDYLYLTRANSFERASE;

AMINO ACID BLOOD LEVEL; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARABIDOPSIS; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ENZYME BINDING; GLYCOSYLATION; HUMAN; HYDROPHOBICITY; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN STRUCTURE; REGULATORY MECHANISM; REVIEW; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS;

ANIMALS; HUMANS; NUCLEOTIDYLTRANSFERASES; PHYLOGENY; PLANT EXTRACTS; PLANT PROTEINS; STRUCTURAL HOMOLOGY, PROTEIN; URIDINE DIPHOSPHATE SUGARS; UTP-GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE;

EID: 80054051304     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20110730     Document Type: Review

References (49)

1. Reiter, W. D. (2008) Biochemical genetics of nucleotide sugar interconversion reactions. Curr. Opin. Plant Biol. 11, 236-243
2. Kotake, T., Hirosawa, C., Ando, Y. and Tsumuraya, Y. (2010) Generation of nucleotide sugars for biomass formation in plants. Plant Biotechnol. 27, 231-236
3. Johansson, H., Sterky, F., Amini, B., Lundeberg, J. and Kleczkowski, L. A. (2002) Molecular cloning and characterization of a cDNA encoding poplar UDP-glucose dehydrogenase, a key gene of hemicellulose/pectin formation. Biochim. Biophys. Acta 1576, 53-58 (Pubitemid 34597084)
4. Kleczkowski, L. A., Kunz, S. and Wilczynska, M. (2010) Mechanisms of UDP-glucose synthesis in plants. Crit. Rev. Plant Sci. 29, 191-203
5. Kotake, T., Yamaguchi, D., Ohzono, H., Hojo, S., Kaneko, S., Ishida, H. K. and Tsumuraya, Y. (2004) UDP-sugar pyrophosphorylase with broad substrate specificity toward various monosaccharide 1-phosphates from pea sprouts. J. Biol. Chem. 279, 45728-45736 (Pubitemid 39491563)
6. Kotake, T., Hojo, S., Yamaguchi, D., Aohara, T., Konishi, T. and Tsumuraya, Y. (2007) Properties and physiological functions of UDP-sugar pyrophosphorylase in Arabidopsis. Biosci. Biotechnol. Biochem. 71, 761-77
7. Litterer, L. A., Plaisance, K. L., Schnurr, J. A., Storey, K. K., Jung, H.J.G., Gronwald, J. W. and Somers, D. A. (2006) Biosynthesis of UDP-glucuronic acid in developing soybean embryos: possible role of UDP-sugar pyrophosphorylase. Physiol. Plant. 128, 200-211 (Pubitemid 44401099)
8. Litterer, L. A., Schnurr, J. A., Plaisance, K. L., Storey, K. K., Gronwald, J. W. and Somers, D. A. (2006) Characterization and expression of Arabidopsis UDP-sugar pyrophosphorylase. Plant Physiol. Biochem. 44, 171-180 (Pubitemid 44202513)
9. Damerow, S., Lamerz, A. C., Haselhorst, T., Fuhring, J., Zarnovican, P., von Itzstein, M. and Routier, F. H. (2010) Leishmania UDP-sugar pyrophosphorylase: the missing link in galactose salvage? J. Biol. Chem. 285, 878-887
10. Yang, T. and Bar-Peled, M. (2010) Identification of a novel UDP-sugar pyrophosphorylase with a broad substrate specificity in Trypanosoma cruzi. Biochem. J. 429, 533-543
11. Kleczkowski, L. A., Decker, D. and Wilczynska, M. (2011) UDP-sugar pyrophosphorylase: a new old mechanism for sugar activation. Plant Physiol. 156, 3-10
12. Wang-Gillam, A., Pastuszak, I., Stewart, M., Drake, R. R. and Elbein, A. D. (2000) Identification and modification of the uridine-binding site of the UDP-GalNAc (GlcNAc) pyrophosphorylase. J. Biol. Chem. 275, 1433-1438 (Pubitemid 30051203)
13. Peneff, C., Ferrari, P., Charrier, V., Taburet, Y., Monnier, C., Zamboni, V., Winter, J., Harnois, M., Fassy, F. and Bourne, Y. (2001) Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture. EMBO J. 20, 6191-6202 (Pubitemid 33078693)
14. Yang, T., Echols, M., Martin, A. and Bar-Peled, M. (2010) Identification and characterization of a strict and of a promiscuous N-acetylglucosamine-1-P uridylyltransferase in Arabidopsis. Biochem. J. 430, 275-284
15. Kleczkowski, L. A. (1999) A phosphoglycerate to inorganic phosphate ratio is the major factor in controlling starch levels in chloroplasts via ADP-glucose pyrophosphorylase regulation. FEBS Lett. 448, 153-156
16. Lamerz, A. C., Haselhorst, T., Bergfeld, A. K., von Itzstein, M. and Gerardy-Schahn, R. (2006) Molecular cloning of the Leishmania major UDP-glucose pyrophosphorylase, functional characterization, and ligand binding analyses using NMR spectroscopy. J. Biol. Chem. 281, 16314-16322
17. McCoy, J. G., Bitto, E., Bingman, C. A., Wesenberg, G. E., Bannen, R. M., Kondrashov, D. A. and Phillips, G. N. (2007) Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP. J. Mol. Biol. 366, 830-841 (Pubitemid 46175866)
18. Maruyama, D., Nishitani, Y., Nonaka, T., Kita, A., Fukami, T. A., Mio, T., Yamada-Okabe, H., Yamada-Okabe, T. and Miki, K. (2007) Crystal structure of uridine-diphospho- N-acetylglucosamine pyrophosphorylase from Candida albicans and catalytic reaction mechanism. J. Biol. Chem. 282, 17221-17230 (Pubitemid 47093203)
19. Steiner, T., Lamerz, A. C., Hess, P., Breithaupt, C., Krapp, S., Bourenkov, G., Huber, R., Gerardy-Schahn, R. and Jacob, U. (2007) Open and closed structures of the UDP-glucose pyrophosphorylase from Leishmania major . J. Biol. Chem. 282, 13003-13010 (Pubitemid 47100592)
20. Okazaki, Y., Shimojima, M., Sawada, Y., Toyooka, K., Narisawa, T., Mochida, K., Tanaka, H., Matsuda, F., Hirai, A., Hirai, M. Y. et al. (2009) A chloroplastic UDP-glucose pyrophosphorylase from Arabidopsis is the committed enzyme for the first step of sulfolipid biosynthesis. Plant Cell 21, 892-909
21. Dickmanns, A., Damerow, S., Neumann, P., Schulz, E. C., Lamerz, A. C., Routier, F. H. and Ficner, R. (2011) Structural basis for the broad substrate range of the UDP-sugar pyrophosphorylase from Leishmania major. J. Mol. Biol. 405, 461-478
22. Meng, M., Wilczynska, M. and Kleczkowski, L. A. (2008) Molecular and kinetic characterization of two UDP-glucose pyrophosphorylases, products of distinct genes, from Arabidopsis. Biochim. Biophys. Acta 1784, 967-972
23. Schnurr, J. A., Storey, K. K., Jung, H.J.G., Somers, D. A. and Gronwald, J. W. (2006) UDP-sugar pyrophosphorylase is essential for pollen development in Arabidopsis. Planta 224, 520-532 (Pubitemid 44188097)
24. Chen, R., Zhao, X., Shao, Z., Wei, Z., Wang, Y., Zhu, L., Zhao, J., Sun, M., He, R. and He, G. (2007) Rice UDP-glucose pyrophosphorylase1 is essential for pollen callose deposition, and its cosuppression results in a new type of thermosensitive genic male sterility. Plant Cell 19, 847-861 (Pubitemid 46953232)
25. Meng, M., Geisler, M., Johansson, H., Harholt, J., Scheller, H. V., Mellerowicz, E. J. and Kleczkowski, L. A. (2009) UDP-glucose pyrophosphorylase is not rate-limiting, but is essential in Arabidopsis. Plant Cell Physiol. 50, 998-1011
26. Park, J. I., Ishimizu, T., Suwabe, K., Sudo, K., Masuko, H., Hakozaki, H., Nou, I. S., Suzuki, G. and Watanabe, M. (2010) UDP-glucose pyrophosphorylase is rate limiting in vegetative and reproductive phases in Arabidopsis thaliana . Plant Cell Physiol. 51, 981-996
27. Chang, C. W., Moseley, J. L., Wykoff, D. and Grossman, A. R. (2005) The LPB1 gene is important for acclimation of Chlamydomonas reinhardtii to phosphorus and sulfur deprivation. Plant Physiol. 138, 319-329 (Pubitemid 43138131)
28. Wehrli, S., Reynolds, R. and Segal, S. (2007) Evidence for function of UDP galactose pyrophosphorylase in mice with absent galactose-1-phosphate uridyltransferase. Mol. Genet. Metab. 91, 191-194 (Pubitemid 46765174)
29. Knop, J. K. and Hansen, R. G. (1970) Uridine diphosphate glucose pyrophosphorylase: crystallization and properties of the enzyme from human liver. J. Biol. Chem. 245, 2499-2504
30. Geisler, M., Wilczynska, M., Karpinski, S. and Kleczkowski, L. A. (2004) Toward a blueprint for UDP-glucose pyrophosphorylase structure/ function properties: homology-modeling analyses. Plant Mol. Biol. 56, 783-794 (Pubitemid 40580425)
31. Dunbrack, R. L. (2006) Sequence comparison and protein structure prediction. Curr. Opin. Struct. Biol. 16, 374-384
32. McCleverty, C. J., Hornsby, M., Spraggon, G. and Kreusch, A. (2007) Crystal structure of human Pus10, a novel pseudouridine synthase. J. Mol. Biol. 373, 1243-54 (Pubitemid 47539484)
33. Roberts, E., Eargle, J., Wright, D. and Luthey-Schulten, Z. (2006) MultiSeq: unifying sequence and structure data for evolutionary analysis. BMC Bioinformatics 7, 382
34. Roeben, A., Plitzko, J. M., Körner, R., Bottcher, U.M.K., Siegers, K., Hayer-Hartl, M. and Bracher, A. (2006) Structural basis for subunit assembly in UDP-glucose pyrophosphorylase from Saccharomyces cerevisiae. J. Mol. Biol. 364, 551-560 (Pubitemid 44755314)
35. Wang-Gillam, A., Pastuszak, I. and Elbein, A. D. (1998) A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc. J. Biol. Chem. 273, 27055-27057 (Pubitemid 28500408)
36. Meng, M., Fitzek, E., Gajowniczek, A., Wilczynska, M. and Kleczkowski, L. A. (2009) Domain-specific determinants of catalysis/substrate binding and the oligomerization status of barley UDP-glucose pyrophosphorylase. Biochim. Biophys. Acta 1794, 1734-1742
37. Katsube, T., Kazuta, Y., Tanizawa, K. and Fukui, T. (1991) Expression in Escherichia coli of UDP-glucose pyrophosphorylase cDNA from potato tuber and functional assessment of the lysyl residues located at the substrate-binding site. Biochemistry 30, 8546-8551
38. Martz, F., Wilczynska, M. and Kleczkowski, L. A. (2002) Oligomerization status, with the monomer as active species, defines catalytic efficiency of UDP-glucose pyrophosphorylase. Biochem. J. 367, 295-300 (Pubitemid 35176918)
39. Kleczkowski, L. A., Martz, F. and Wilczynska, M. (2005) Factors affecting oligomerization status of UDP-glucose pyrophosphorylase. Phytochemistry 66, 2815-2821 (Pubitemid 41719189)
40. Gandhi, T.K.B., Zhong, J., Mathivanan, S., Karthick, L., Chandrika, K. N., Mohan, S. S., Sharma, S., Pinkert, S., Nagaraju, S., Periaswamy, B. et al. (2006) Analysis of the human protein interactome and comparison with yeast, worm and fly interaction datasets. Nat. Genet. 38, 285-293
41. Kleczkowski, L. A., Geisler, M., Ciereszko, I. and Johansson, H. (2004) UDP-glucose pyrophosphorylase. an old protein with new tricks. Plant Physiol. 134, 912-918 (Pubitemid 38398240)
42. Kim, H., Choi, J., Kim, T., Lokanath, N. K., Ha, S. C., Suh, S. W., Hwang, H. Y. and Kim, K. K. (2010) Structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase. Mol. Cells 29, 397-405
43. Lai, X., Wu, J., Chen, S., Zhang, X. and Wang, H. (2008) Expression, purification, and characterization of a functionally active Mycobacterium tuberculosis UDP-glucose pyrophosphorylase. Protein Expr. Purif. 61, 50-56
44. Bosco, M. B., Machtey, M., Iglesias, A. A. and Aleanzi, M. (2009) UDPglucose pyrophosphorylase from Xanthomonas spp. Characterization of the enzyme kinetics, structure and inactivation related to oligomeric dissociation. Biochimie 91, 204-213
45. von Itzstein, M. (2008) Disease-associated carbohydrate-recognising proteins and structure-based inhibitor design. Curr. Opin. Struct. Biol. 18, 558-566
46. Reynès, C., Host, H., Camproux, A. C., Laconde, G., Leroux, F., Mazars, A., Deprez, B., Fahraeus, R., Villoutreix, B. O. and Sperandio, O. (2010) Designing focused chemical libraries enriched in protein-protein interaction inhibitors using machine-learning methods. PLoS Comput. Biol. 6, e1000695
47. Kleczkowski, L. A. (1994) Inhibitors of photosynthetic enzymes/carriers and metabolism. Annu. Rev. Plant Physiol. Plant Mol. Biol. 45, 339-367
48. Bates, P. A., Kelley, L. A., MacCallum, R. M. and Sternberg, M.J.E. (2001) Enhancement of protein modeling by human intervention in applying the automatic programs 3D jigsaw and 3D PSSM. Proteins 5 (Suppl.), 39-46 (Pubitemid 34113166)
49. Humphrey, W., Dalke, A. and Schulten, K. (1996) VMD: Visual Molecular Dynamics. J. Mol. Graph. 14, 33-38 (Pubitemid 26152973)