Home Ricerca Sedi Chi siamo Organigramma Personale Contatti Didattica Login Documenti EN
Progetti in evidenza
(Link esterno)

(1204 visite)

Fondo Europeo Pesca
(614 visite)

(Link esterno)

Fondazione Veronesi
(Link esterno)

(1082 visite)

(1179 visite)

(Link esterno)

(1320 visite)

(1083 visite)

(1025 visite)

MFAG Grant
(1126 visite)

(Link esterno)


Contiene: [X]      Estesa     Autori: [X]  Tipo di lavoro: [X]
Data iniziale: Data finale: [X]      Sede: Affiliazione IBB     
[Pulisci modulo]

Probing the activity of diguanylate cyclases and c-di-GMP phosphodiesterases in real-time by CD spectroscopy (133 visite)

Stelitano V, Brandt A, Fernicola S, Franceschini S, Giardina G, Pica A, Rinaldo S, Sica F, Cutruzzola F

Nucleic Acids Res (ISSN: 0305-1048, 0305-5104, 1362-4962), 2013 Apr; 41(7): e79-e79.

Tipo di articolo: Journal Article, Abstract, Conference, Research Support, Non-U. S. Gov'T, , Impact factor: 4.188, Impact factor a 5 anni: 7.163, Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84876543297&partnerID=40&md5=de1331fe5198c9ad7a72605c1a4cb7aa

Parole chiave: Cyclic Diguanylic Acid, Cyclic Adenilic Acid, Cyclic Gmp Phosphodiesterase, Diguanylate Cyclase, Dimer, Guanine, Manganese, Unclassified Drug, Article, Biofilm, Catalysis, Circular Dichroism, Concentration (parameters), Controlled Study, Intercalation Complex, Nonhuman, Priority Journal, Ultraviolet Radiation, -Cyclic-Gmp Phosphodiesterases, Models, Molecular, Metabolism, Methods, Analogs, Derivatives, Chemistry,

Affiliazioni: *** IBB - CNR ***
Istituto Pasteur-Fondazione Cenci Bolognetti, Department of Biochemical Sciences, Sapienza University of Rome, 00185 Rome, Italy
Department of Chemical Sciences, University of Naples Federico II, 80126 Naples, Italy
Institute of Biostructure and Bioimaging, CNR, 80134 Naples, Italy

Riferimenti: Jenal, U., Malone, J., Mechanisms of cyclic-di-GMP signaling in bacteria (2006) Annual Review of Genetics, 40, pp. 385-407. , DOI 10. 1146/annurev. genet. 40. 110405. 09042

Hengge, R., Principles of c-di-GMP signalling in bacteria (2009) Nat. Rev. Microbiol, 7, pp. 263-273

Ryan, R. P., Tolker-Nielsen, T., Dow, J. M., When the PilZ don't work: Effectors for cyclic di-GMP action in bacteria (2012) Trends Microbiol, 20, pp. 235-242

Zhang, Z., Gaffney, B. L., Jones, R. A., C-di-GMP displays A monovalent metal ion-dependent polymorphism (2004) Journal of the American Chemical Society, 126 (51), pp. 16700-16701. , DOI 10. 1021/ja0449832

Zhang, Z., Kim, S., Gaffney, B. L., Jones, R. A., Polymorphism of the signaling molecule c-di-GMP (2006) Journal of the American Chemical Society, 128 (21), pp. 7015-7024. , DOI 10. 1021/ja0613714

Gentner, M., Allan, M. G., Zaehringer, F., Schirmer, T., Grzesiek, S., Oligomer Formation of the bacterial second messenger c-di-GMP: Reaction rates and equilibrium constants indicate a monomeric state at physiological concentrations (2012) J. Am. Chem. Soc, 134, pp. 1019-1029

Nakayama, S., Kelsey, I., Wang, J., Roelofs, K., Stefane, B., Luo, Y., Lee, V. T., Sintim, H. O., Thiazole orange-induced c-di-GMP quadruplex formation facilitates a simple fluorescent detection of this ubiquitous biofilm regulating molecule (2011) J. Am. Chem. Soc, 133, pp. 4856-4864

Ko, J., Ryu, K. S., Kim, H., Shin, J. S., Lee, J. O., Cheong, C., Choi, B. S., Structure of PP4397 reveals the molecular basis for different c-di-GMP binding modes by Pilz domain proteins (2010) J. Mol. Biol, 398, pp. 97-110

Benach, J., Swaminathan, S. S., Tamayo, R., Handelman, S. K., Folta-Stogniew, E., Ramos, J. E., Forouhar, F., Hunt, J. F., The structural basis of cyclic diguanylate signal transduction by PilZ domains (2007) EMBO Journal, 26 (24), pp. 5153-5166. , DOI 10. 1038/sj. emboj. 7601918, PII 7601918

Duvel, J., Bertinetti, D., Moller, S., Schwede, F., Morr, M., Wissing, J., Radamm, L., Jansch, L., A chemical proteomics approach to identify c-di-GMP binding proteins in Pseudomonas aeruginosa (2012) J. Microbiol. Methods, 88, pp. 229-236

Yang, C. Y., Chin, K. H., Chuah, M. L., Liang, Z. X., Wang, A. H., Chou, S. H., The structure and inhibition of a GGDEF diguanylate cyclase complexed with (c-di-GMP) (2) at the active site (2011) Acta Crystallogr. D Biol. Crystallogr, 67, pp. 997-1008

De, N., Pirruccello, M., Krasteva, P. V., Bae, N., Raghavan, R. V., Sondermann, H., Phosphorylation-independent regulation of the diguanylate cyclase WspR (2008) PLoS Biol, 6, pp. e67

Chan, C., Paul, R., Samoray, D., Amiot, N. C., Giese, B., Jenal, U., Schirmer, T., Structural basis of activity and allosteric control of diguanylate cyclase (2004) Proceedings of the National Academy of Sciences of the United States of America, 101 (49), pp. 17084-17089. , DOI 10. 1073/pnas. 0406134101

Minasov, G., Padavattan, S., Shuvalova, L., Brunzelle, J. S., Miller, D. J., Basle, A., Massa, C., Anderson, W. F., Crystal structures of YkuI and its complex with second messenger cyclic Di-GMP suggest catalytic mechanism of phosphodiester bond cleavage by EAL domains (2009) J. Biol. Chem, 284, pp. 13174-13184

Navarro, M. V., De, N., Bae, N., Wang, Q., Sondermann, H., Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX (2009) Structure, 17, pp. 1104-1116

Wang, J., Zhou, J., Donaldson, G. P., Nakayama, S., Yan, L., Lam, Y. F., Lee, V. T., Sintim, H. O., Conservative change to the phosphate moiety of cyclic diguanylic monophosphate remarkably affects its polymorphism and ability to bind DGC, PDE, and PilZ proteins (2011) J. Am. Chem. Soc, 133, pp. 9320-9330

Paul, R., Weiser, S., Amiot, N. C., Chan, C., Schirmer, T., Giese, B., Jenal, U., Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain (2004) Genes and Development, 18 (6), pp. 715-727. , DOI 10. 1101/gad. 289504

Paul, R., Abel, S., Wassmann, P., Beck, A., Heerklotz, H., Jenal, U., Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization (2007) Journal of Biological Chemistry, 282 (40), pp. 29170-29177. , http: //www. jbc. org/cgi/reprint/282/40/29170, DOI 10. 1074/jbc. M704702200

Christen, B., Christen, M., Paul, R., Schmid, F., Folcher, M., Jenoe, P., Meuwly, M., Jenal, U., Allosteric control of cyclic di-GMP signaling (2006) Journal of Biological Chemistry, 281 (42), pp. 32015-32024. , http: //www. jbc. org/cgi/reprint/281/42/32015, DOI 10. 1074/jbc. M603589200

Tuckerman, J. R., Gonzalez, G., Sousa, E. H., Wan, X., Saito, J. A., Alam, M., Gilles-Gonzalez, M. A., An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control (2009) Biochemistry, 48, pp. 9764-9774

Neunuebel, M. R., Golden, J. W., The Anabaena sp. strain PCC 7120 gene all2874 encodes a diguanylate cyclase and is required for normal heterocyst development under high-light growth conditions (2008) J. Bacteriol, 190, pp. 6829-6836

Christen, M., Christen, B., Folcher, M., Schauerte, A., Jenal, U., Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP (2005) Journal of Biological Chemistry, 280 (35), pp. 30829-30837. , DOI 10. 1074/jbc. M504429200

Sultan, S. Z., Pitzer, J. E., Boquoi, T., Hobbs, G., Miller, M. R., Motaleb, M. A., Analysis of the HD-GYP domain cyclic dimeric GMP phosphodiesterase reveals a role in motility and the enzootic life cycle of Borrelia burgdorferi (2011) Infect. Immun, 79, pp. 3273-3283

Wassmann, P., Chan, C., Paul, R., Beck, A., Heerklotz, H., Jenal, U., Schirmer, T., Structure of BeF3 --Modified Response Regulator PleD: Implications for Diguanylate Cyclase Activation, Catalysis, and Feedback Inhibition (2007) Structure, 15 (8), pp. 915-927. , DOI 10. 1016/j. str. 2007. 06. 016, PII S0969212607002493

Lai, T. H., Kumagai, Y., Hyodo, M., Hayakawa, Y., Rikihisa, Y., The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic Di-GMP in host cell infection (2009) J. Bacteriol, 191, pp. 693-700

Sawai, H., Yoshioka, S., Uchida, T., Hyodo, M., Hayakawa, Y., Ishimori, K., Aono, S., Molecular oxygen regulates the enzymatic activity of a heme-containing diguanylate cyclase (HemDGC) for the synthesis of cyclic di-GMP (2010) Biochim. Biophys. Acta, 1804, pp. 166-172

Rao, F., Pasunooti, S., Ng, Y., Zhuo, W., Lim, L., Liu, A. W., Liang, Z. X., Enzymatic synthesis of c-di-GMP using a thermophilic diguanylate cyclase (2009) Anal. Biochem, 389, pp. 138-142

He, Y. W., Boon, C., Zhou, L., Zhang, L. H., Co-regulation of Xanthomonas campestris virulence by quorum sensing and a novel two-component regulatory system RavS/RavR (2009) Mol. Microbiol, 71, pp. 1464-1476

Rao, F., Yang, Y., Qi, Y., Liang, Z. X., Catalytic mechanism of cyclic di-GMP-specific phosphodiesterase: A study of the EAL domain-containing RocR from Pseudomonas aeruginosa (2008) J. Bacteriol, 190, pp. 3622-3631

Barends, T. R., Hartmann, E., Griese, J. J., Beitlich, T., Kirienko, N. V., Ryjenkov, D. A., Reinstein, J., Schlichting, I., Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase (2009) Nature, 459, pp. 1015-1018

Rao, F., Qi, Y., Chong, H. S., Kotaka, M., Li, B., Li, J., Lescar, J., Liang, Z. X., The functional role of a conserved loop in EAL domain-based cyclic di-GMP-specific phosphodiesterase (2009) J. Bacteriol, 191, pp. 4722-4731

Yang, F., Tian, F., Sun, L., Chen, H., Wu, M., Yang, C. H., He, C., A novel two-component system PdeK/PdeR regulates c-di-GMP turnover and virulence of Xanthomonas oryzae pv. oryzae (2012) Mol. Plant Microbe Interact, 25, pp. 1361-1369

Ryan, R. P., Fouhy, Y., Lucey, J. F., Crossman, L. C., Spiro, S., He, Y. W., Zhang, L. H., Williams, P., Cell-cell signaling in Xanthomonas campestris involves an HD-GYP domain protein that functions in cyclic di-GMP turnover (2006) Proc. Natl Acad. Sci. USA, 103, pp. 6712-6717

Sharma, I. M., Dhanaraman, T., Mathew, R., Chatterji, D., Synthesis and Characterization of a fluorescent analogue of cyclic di-GMP (2012) Biochemistry, 51, p. 5443

Egli, M., Gessner, R. V., Williams, L. D., Quigley, G. J., Van Der Marel, G. A., Van Boom, J. H., Rich, A., Frederick, C. A., Atomic-resolution structure of the cellulose synthase regulator cyclic diguanylic acid (1990) Proc. Natl Acad. Sci. USA, 87, pp. 3235-3239

Altomare, A., Burla, M. C., Camalli, M., Cascarano, G. L., Giacovazzo, C., Guagliardi, A., Moliterni, A. G. G., Spagna, R., SIR97: A new tool for crystal structure determination and refinement (1999) Journal of Applied Crystallography, 32 (1), pp. 115-119

Sheldrick, G. M., A short history of SHELX (2008) Acta Crystallogr. A, 64, pp. 112-122

Kelly, S. M., Price, N. C., The use of circular dichroism in the investigation of protein structure and function (2000) Curr. Protein Pept. Sci, 1, pp. 349-384

Liaw, Y. -C., Gao, Y. -G., Robinson, H., Sheldrick, G. M., Sliedregt, L. A. J. M., Van Der Marel, G. A., Van Boom, J. H., Wang, A. H. -J., Cyclic diguanylic acid behaves as a host molecule for planar intercalators (1990) FEBS Letters, 264 (2), pp. 223-227. , DOI 10. 1016/0014-5793 (90) 80253-F

Zhang, Y., Huang, K., On the interactions of hydrated metal cations (Mg2+, Mn2+, Ni2+, Zn2+) with guanine-cytosine Watson-Crick and guanine-guanine reverse-Hoogsteen DNA base pairs (2007) J. Mol. Struct. THEOCHEM, 812, pp. 51-62

Eichhorn, G. L., Shin, Y. A., Interaction of metal ions with polynucleotides and related compounds: Part XII. The relative effect of various metal ions on DNA helicity (1968) J. Am. Chem. Soc, 90, pp. 7323-7328

Solt, I., Simon, I., Csaszar, A. G., Fuxreiter, M., Electrostatic versus nonelectrostatic effects in DNA sequence discrimination by divalent ions Mg2+ and Mn2+ (2007) Journal of Physical Chemistry B, 111 (22), pp. 6272-6279. , DOI 10. 1021/jp0668192

Sponer, J. E., Sychrovsky, V., Hobza, P., Sponer, J., Interactions of hydrated divalent metal cations with nucleic acid bases. How to relate the gas phase data to solution situation and binding selectivity in nucleic acids (2004) Phys. Chem. Chem. Phys, 6, pp. 2772-2780

Antoniani, D., Bocci, P., MacIag, A., Raffaelli, N., Landini, P., Monitoring of diguanylate cyclase activity and of cyclic-di-GMP biosynthesis by whole-cell assays suitable for high-throughput screening of biofilm inhibitors (2009) Appl. Microbiol. Biotechnol, 85, pp. 1095-1104

Malone, J. G., Jaeger, T., Manfredi, P., Dotsch, A., Blanka, A., Bos, R., Cornelis, G. R., Jenal, U., The YfiBNR signal transduction mechanism reveals novel targets for the evolution of persistent Pseudomonas aeruginosa in cystic fibrosis airways (2012) PLoS Pathog, 8, pp. e1002760

Massie, J. P., Reynolds, E. L., Koestler, B. J., Cong, J. P., Agostoni, M., Waters, C. M., Quantification of high-specificity cyclic diguanylate signaling (2012) Proc. Natl Acad. Sci. USA, 109, pp. 12746-12751

Bacteria react to adverse environmental stimuli by clustering into organized communities called biofilms. A remarkably sophisticated control system based on the dinucleotide 3 -5 cyclic diguanylic acid (c-di-GMP) is involved in deciding whether to form or abandon biofilms. The ability of c-di-GMP to form self-intercalated dimers is also thought to play a role in this complex regulation. A great advantage in the quest of elucidating the catalytic properties of the enzymes involved in c-di-GMP turnover (diguanylate cyclases and phosphodiesterases) would come from the availability of an experimental approach for in vitro quantification of c-di-GMP in real-time. Here, we show that c-di-GMP can be detected and quantified by circular dichroism (CD) spectroscopy in the low micromolar range. The method is based on the selective ability of manganese ions to induce formation of the intercalated dimer of the c-di-GMP dinucleotide in solution, which displays an intense sigmoidal CD spectrum in the near-ultraviolet region. This characteristic spectrum originates from the stacking interaction of the four mutually intercalated guanines, as it is absent in the other cyclic dinucleotide 3 -5 cyclic adenilic acid (c-di-AMP). Thus, near-ultraviolet CD can be used to effectively quantify in real-time the activity of diguanylate cyclases and phosphodiesterases in solution. 2013 The Author (s)
Nessun risultato.
Nessun risultato.

Contiene: [X]      Estesa     Autori: [X]  Tipo di lavoro: [X]
Data iniziale: Data finale: [X]      Sede: Affiliazione IBB     
[Pulisci modulo]

Puglisi A, Tabbì G, Vecchio G
* Bioconjugates of cyclodextrins of manganese salen-type ligand with superoxide dismutase activity (87 visite)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2004 Jun; 98(6): 969-976.
Impact Factor: 2.225
Dettagli    Esporta in BibTeX    Esporta in EndNote

1 Records (1 escludendo Abstract e Conferenze).
Impact factor totale: 2.225 (2.225 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 3.452 (3.452 escludendo Abstract e Conferenze).

    Esporta in BibTeX    Esporta in EndNote

Ultima modifica di Marco Comerci in data Friday 16 March 2018, 12:13:59
133 visite. Ultima visita in data Sunday 09 December 2018, 17:20:00

Webmaster and developer: Marco Comerci
Per problemi e suggerimenti: adminibb.cnr.it
Ultimo aggiornamento: Tuesday 11 December 2018, 12:37:42