DUTPases, the unexplored family of signalling molecules

Current Opinion in Microbiology

Volumn 16, Issue 2, 2013, Pages 163-170

  Penadés, José R ^a,b   Donderis, Jorge ^a,c   García Caballer, María ^b   Tormo Más, María Ángeles ^d   Marina, Alberto ^a,c  

^a INSTITUTO DE BIOMEDICINA DE VALENCIA   (Spain)

^b UNIVERSIDAD CEU CARDENAL HERRERA   (Spain)

^c CENTRO DE INVESTIGACIÓN BIOMÉDICA EN RED DE ENFERMEDADES RARAS CIBERER   (Spain)

^d INSTITUTO VALENCIANO DE INVESTIGACIONES AGRARIAS IVIA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; INTERLEUKIN 10; INTERLEUKIN 1BETA; INTERLEUKIN 6; INTERLEUKIN 8; MYELOID DIFFERENTIATION FACTOR 88; TOLL LIKE RECEPTOR 2; TUMOR NECROSIS FACTOR ALPHA; VIRULENCE FACTOR;

CAENORHABDITIS ELEGANS; CAMPYLOBACTER JEJUNI; CATALYSIS; DROSOPHILA MELANOGASTER; DROSOPHILA VIRILIS; ENZYME ACTIVITY; ENZYME STRUCTURE; EPSTEIN BARR VIRUS; ESCHERICHIA COLI; EUKARYOTIC CELL; GENOTYPE; HERPES VIRUS; HUMAN; HYDROLYSIS; IMMUNOREGULATION; KAPOSI SARCOMA; LEISHMANIA MAJOR; LIGAND BINDING; MACROPHAGE; MONOCYTE; MUTAGENESIS; MYCOBACTERIUM LEPRAE; MYCOBACTERIUM SMEGMATIS; MYCOBACTERIUM TUBERCULOSIS; NATURAL KILLER CELL; NONHUMAN; NUCLEOTIDE SEQUENCE; PATHOGENICITY; PATHOGENICITY ISLAND; PROKARYOTIC CELL; PROTEIN FAMILY; REVIEW; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS PHAGE; TRYPANOSOMA CRUZI; UPREGULATION; VIRUS REPLICATION;

DEOXYURACIL NUCLEOTIDES; EUKARYOTIC CELLS; GENE EXPRESSION REGULATION; PROKARYOTIC CELLS; PYROPHOSPHATASES; SIGNAL TRANSDUCTION;

EUKARYOTA; PROKARYOTA;

EID: 84877028591     PISSN: 13695274     EISSN: 18790364     Source Type: Journal    
DOI: 10.1016/j.mib.2013.02.005     Document Type: Review

References (41)

1. Vértessy B.G., Tóth J. Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases. Acc Chem Res 2009, 42:97-106.
2. Kouzminova E.A., Kuzminov A. Chromosomal fragmentation in dUTPase-deficient mutants of Escherichia coli and its recombinational repair. Mol Microbiol 2004, 51:1279-1295.
3. Tchigvintsev A., Singer A.U., Flick R., Petit P., Brown G., Evdokimova E., Savchenko A., Yakunin A.F. Structure and activity of the Saccharomyces cerevisiae dUTP pyrophosphatase DUT1, an essential housekeeping enzyme. Biochem J 2011, 437:243-253.
4. Whittingham J.L., Leal I., Nguyen C., Kasinathan G., Bell E., Jones A.F., Berry C., Benito A., Turkenburg J.P., Dodson E.J., et al. dUTPase as a platform for antimalarial drug design: structural basis for the selectivity of a class of nucleoside inhibitors. Structure 2005, 13:329-338.
5. Koehler S.E., Ladner R.D. Small interfering RNA-mediated suppression of dUTPase sensitizes cancer cell lines to thymidylate synthase inhibition. Mol Pharmacol 2004, 66:620-626.
6. Maul R.W., Gearhart P.J. AID and somatic hypermutation. Adv Immunol 2010, 105:159-191.
7. Yan N., O'Day E., Wheeler L.A., Engelman A., Lieberman J. HIV DNA is heavily uracilated, which protects it from autointegration. Proc Natl Acad Sci U S A 2011, 108:9244-9249.
8. Muha V., Horváth A., Békési A., Pukáncsik M., Hodoscsek B., Merényi G., Róna G., Batki J., Kiss I., Jankovics F., et al. Uracil-containing DNA in Drosophila: stability, stage-specific accumulation, and developmental involvement. PLoS Genet 2012, 8:e1002738.
9. Cedergren-Zeppezauer E.S., Larsson G., Nyman P.O., Dauter Z., Wilson K.S. Crystal structure of a dUTPase. Nature 1992, 355:740-743.
10. Mol C.D., Harris J.M., McIntosh E.M., Tainer J.A. Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits. Structure 1996, 4:1077-1092.
11. Vertessy B.G., Larsson G., Persson T., Bergman A.C., Persson R., Nyman P.O. The complete triphosphate moiety of non-hydrolyzable substrate analogues is required for a conformational shift of the flexible C-terminus in E. coli dUTP pyrophosphatase. FEBS Lett 1998, 421:83-88.
12. Varga B., Barabás O., Kovári J., Tóth J., Hunyadi-Gulyás é., Klement é., Medzihradszky K.F., Tölgyesi F., Fidy J., Vértessy B.G. Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase. FEBS Lett 2007, 581:4783-4788.
13. Freeman L., Buisson M., Tarbouriech N., Van der Heyden A., Labbe P., Burmeister W.P. The flexible motif V of Epstein-Barr virus deoxyuridine 5'-triphosphate pyrophosphatase is essential for catalysis. J Biol Chem 2009, 284:25280-25289.
14. Pécsi I., Szabó J.E., Adams S.D., Simon I., Sellers J.R., Vértessy B.G., Tóth J. Nucleotide pyrophosphatase employs a P-loop-like motif to enhance catalytic power and NDP/NTP discrimination. Proc Natl Acad Sci U S A 2011, 108:14437-14442.
15. Moroz O.V., Harkiolaki M., Galperin M.Y., Vagin A.A., González-Pacanowska D., Wilson K.S. The crystal structure of a complex of Campylobacter jejuni dUTPase with substrate analogue sheds light on the mechanism and suggests the " basic module" for dimeric d(C/U)TPases. J Mol Biol 2004, 342:1583-1597.
16. Hemsworth G.R., Moroz O.V., Fogg M.J., Scott B., Bosch-Navarrete C., González-Pacanowska D., Wilson K.S. The crystal structure of the Leishmania major deoxyuridine triphosphate nucleotidohydrolase in complex with nucleotide analogues, dUMP, and deoxyuridine. J Biol Chem 2011, 286:16470-16481.
17. Tarbouriech N., Buisson M., Seigneurin J.-M., Cusack S., Burmeister W.P. The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases. Structure 2005, 13:1299-1310.
18. Juganaru M., Reina R., Bertolotti L., Stella M.C., Profiti M., Armentano M., Bollo E., Amorena B., Rosati S. In vitro properties of small ruminant lentivirus genotype E. Virology 2011, 410:88-95.
19. Ariza M.-E., Glaser R., Kaumaya P.T.P., Jones C., Williams M.V. The EBV-encoded dUTPase activates NF-kappa B through the TLR2 and MyD88-dependent signaling pathway. J Immunol 2009, 182:851-859.
20. Leang R.S., Wu T.-T., Hwang S., Liang L.T., Tong L., Truong J.T., Sun R. The anti-interferon activity of conserved viral dUTPase ORF54 is essential for an effective MHV-68 infection. PLoS Pathog 2011, 7:e1002292.
21. Madrid A.S., Ganem D. Kaposi's sarcoma-associated herpesvirus ORF54/dUTPase downregulates a ligand for the NK activating receptor NKp44. J Virol 2012, 86:8693-8704.
22. Novick R.P., Christie G.E., Penadés J.R. The phage-related chromosomal islands of Gram-positive bacteria. Nat Rev Microbiol 2010, 8:541-551.
23. úbeda C., Maiques E., Barry P., Matthews A., Tormo M.á., Lasa í., Novick R.P., Penadés J.R. SaPI mutations affecting replication and transfer and enabling autonomous replication in the absence of helper phage. Mol Microbiol 2008, 67:493-503.
24. Tormo M.A., Ferrer M.D., Maiques E., Ubeda C., Selva L., Lasa I., Calvete J.J., Novick R.P., Penadés J.R. Staphylococcus aureus pathogenicity island DNA is packaged in particles composed of phage proteins. J Bacteriol 2008, 190:2434-2440.
25. Tormo-Más M.á., Mir I., Shrestha A., Tallent S.M., Campoy S., Lasa í., Barbé J., Novick R.P., Christie G.E., Penadés J.R. Moonlighting bacteriophage proteins derepress staphylococcal pathogenicity islands. Nature 2010, 465:779-782.
26. Ram G., Chen J., Kumar K., Ross H.F., úbeda C., Damle P.K., Lane K.D., Penadés J.R., Christie G.E., Novick R.P. Staphylococcal pathogenicity island interference with helper phage reproduction is a paradigm of molecular parasitism. Proc Natl Acad Sci U S A 2012, 109:16300-16305.
27. el-Hajj H.H., Zhang H., Weiss B. Lethality of a dut (deoxyuridine triphosphatase) mutation in Escherichia coli. J Bacteriol 1988, 170:1069-1075.
28. Pécsi I., Hirmondo R., Brown A.C., Lopata A., Parish T., Vértessy B.G., Tóth J. The dUTPase enzyme is essential in Mycobacterium smegmatis. PLoS ONE 2012, 7:e37461.
29. Chan S., Segelke B., Lekin T., Krupka H., Cho U.S., Kim M.-Y., So M., Kim C.-Y., Naranjo C.M., Rogers Y.C. Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism. J Mol Biol 2004, 341:503-517.
30. Monot M., Honoré N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A., Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., et al. Comparative genomic and phylogeographic analysis of Mycobacterium leprae. Nat Genet 2009, 41:1282-1289.
31. Muha V., Zagyva I., Venkei Z., Szabad J., Vértessy B.G. Nuclear localization signal-dependent and -independent movements of Drosophila melanogaster dUTPase isoforms during nuclear cleavage. Biochem Biophys Res Commun 2009, 381:271-275.
32. Békési A., Zagyva I., Hunyadi-Gulyás E., Pongrácz V., Kovári J., Nagy A.O., Erdei A., Medzihradszky K.F., Vértessy B.G. Developmental regulation of dUTPase in Drosophila melanogaster. J Biol Chem 2004, 279:22362-22370.
33. Ladner R.D., Caradonna S.J. The human dUTPase gene encodes both nuclear and mitochondrial isoforms. Differential expression of the isoforms and characterization of a cDNA encoding the mitochondrial species. J Biol Chem 1997, 272:19072-19080.
34. Ariza M.-E., Williams M.V. A human endogenous retrovirus K dUTPase triggers a TH1, TH17 cytokine response: does it have a role in psoriasis?. J Investig Dermatol 2011, 131:2419-2427.
35. Behrends C., Sowa M.E., Gygi S.P., Harper J.W. Network organization of the human autophagy system. Nature 2010, 466:68-76.
36. Blagoev B., Kratchmarova I., Ong S.-E., Nielsen M., Foster L.J., Mann M. A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat Biotechnol 2003, 21:315-318.
37. Kim D.-M., Chung K.-S., Choi S.-J., Jung Y.-J., Park S.-K., Han G.-H., Ha J.-S., Song K.-B., Choi N.-S., Kim H.-M., et al. RhoB induces apoptosis via direct interaction with TNFAIP1 in HeLa cells. Int J Cancer 2009, 125:2520-2527.
38. Ewing R.M., Chu P., Elisma F., Li H., Taylor P., Climie S., McBroom-Cerajewski L., Robinson M.D., O'Connor L., Li M., et al. Large-scale mapping of human protein-protein interactions by mass spectrometry. Mol Syst Biol 2007, 3:89.
39. Chu R., Lin Y., Rao M.S., Reddy J.K. Cloning and identification of rat deoxyuridine triphosphatase as an inhibitor of peroxisome proliferator-activated receptor alpha. J Biol Chem 1996, 271:27670-27676.
40. Tormo-Mas M.A., Donderis J., García-Caballer M., Aaron A., Mir-Sanchis I., Marina A., Penades J.R. Phage dUTPases control transfer of virulence genes by a proto-oncogenic G protein-like mechanism. Mol Cell 2013, 49:947-958.
41. Williams D., Norman G., Khoury C., Metcalfe N., Briard J., Laporte A., Sheibani S., Portt L., Mandato C.A., Greenwood M.T. Evidence for a second messenger function of dUTP during Bax mediated apoptosis of yeast and mammalian cells. Biochim Biophys Acta 2011, 1813:315-321.