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7. Abstracts of Selected Posters

Author

Albanese, R., Antoine, J. L., Dutrillaux, B., Ashley, T., Avivi, L., Kariv, I., Barigozzi, C., Baratelli, L., Profeta, S., Bartram, C. R., de Klein, A., Hagemeijer, A., Grosveld, G., Bootsma, D., Bennett, Michael D., Smith, J. B., Ward, J. P., Heslop-Harrison, J. S., Blin, N., Kopun, M., Buys, C. H. C. M., Koerts, T., van der Veen, A. Y., de Leij, L., Civitelli, M. V., Capanna, E., Couturier, J., Arnason, U., Mandahl, N., Créau-Goldberg, N., Turleau, C., Cochet, C., de Grouchy, J., Dietrich, A. J. J., Delhanty, J. D. A., Mazzullo, H. A., Cooke, H. M. G., Dotan, A., Dresser, M. E., Moses, M. J., Evans, E. P., Burgoyne, P. B., Ferraro, M., Lavia, P., Fonatsch, C., Kirchner, H. H., Pajunk, A., Schaadt, M., Burrichter, H., Diehl, V., Ford, J. H., Roberts, C. G., Friebe, B., Vogel, R., Friedländer, M., Gamperl, R., Amtmann, E., Pfister, H., Gebhart, E., Wagner, H., Goetz, P., Chandley, A. C., Speed, R. M., Goyanes, V. J., Schvartzman, J. B., Graeven, U., Weh, H. J., Hossfeld, D. K., Greenblatt, I. M., Gripenberg, U., Söderlund, V., Wahlberg, C., Blomqvist, L., Guichaoua, M. R., Delafontaine, D., Taillemite, J. L., Luciani, J. M., Naaf, T., Grunert, D., Schmid, M., Hameister, H., Sperling, K., Hamers, A., Jongbloet, P., Peeters, G., Geraedts, J., Hartley-Asp, B., Heneen, W. K., Hens, L., Kirsch-Volders, M., Susanne, C., Herbst, E. W., Winking, H., Claussen, C. P., Putz, B., Sellin, D., Kolbus, U., Gropp, A., Bennett, M. D., Heyting, C., Koperdraad, F., Redeker, E. J. W., Holmquist, G., Goldman, M., Jaworska, Halina, Johannisson, R., Kerem, B., Goitein, R., Richier, C., Marcus, M., Cedar, H., Koch, H., Hoehn, H., Kubbies, Manfred, Rabinovitch, Peter S., Kunz, W., Franz, G., Lacadena, J. R., Cermeno, M. C., Orellana, J., Santos, J. L., Lemeunier, F., Derbin, C., Lin, C. C., Hoar, D. I., Hoo, J. J., Macgregor, H. C., Sims, S., Horner, H. A., Pellatt, P., Mackay, J. M., Fox, D. P., Brunt, P. W., Johnston, A. W., Magenis, R. E., Chamberlin, J., Allen, L., Tomar, D., Olson, S., Donlon, T., Marlekaj, P., Balcini, A., Fantoni, A., de Capoa, A., Martinsson, T., Dahllöf, B., Levan, G., Matsukuma, S., Utakoji, T., del Mazo, J., Avila, J., Miller, D. A., Feinstein, S. I., Miller, O. J., Morita, T., Delarbre, C., Gachelin, G., Kourilsky, P., Moritz, K., Moriwaki, K., Miyashita, N., Imai, H. T., Wang, C. H., Bonhomme, F., Murer-Orlando, M., Peterson, A. C., Neitzel, H., Bogenberger, J., Fittler, F., Gaenge, M., Schulze, C., Nietzel, H., Nürnberger, F., Höhn, H., van Ommen, G. J. B., Baas, F., Arnberg, A. C., Pearson, P. L., De Vijilder, J. J. M., Bakker, E., Hofker, M., Wapenaar, M. C., Parrington, J. M., West, L. F., Povey, S., Pasquali, F., Casalone, R., Bernasconi, P., Paul, J., Froster-Iskenius, U., Schwinger, E., Moje, W., Pearson, P. O., Beverstock, G. C., Veenema, H., v.d Kamp, J. J., Petitpierre, E., Philip, J., Lundsteen, C., van der Ploeg, M., van Prooijen-Knegt, A. C., Bauman, J. G. J., van Duijn, P., Puertas, M. J., de la Pena, A., Estades, B., Merino, F., Rao, S. R. V., Vasantha, K., Thelma, B. K., Juyal, R. C., Jhanwar, S. C., Ratomponirina, Ch, Hamilton, A., Rumpler, Y., Moses, M., Raveh, D., Ben-Zeoev, A., Redi, C. A., Garagna, S., Italy, C. N. R., Robert-Nicoud, M., Streichhan, I., Möhr, E., Westermann, R., Grossbach, U., Sandberg, P., Levan, A., Schäfer, Mireille, Schempp, W., Scheres, J. M. J. C., Hustinx, T. W. J., Holdrinet, R. S. G., Tice, R. R., Schwarzacher, T., Finch, R. A., Searle, J. B., Sharma, T., Sen, S., Cheong, N., Siebert, E., Loidl, J., Slater, R. M., de Kraker, J., Voute, P. A., Delemarre, J. F. M., Smeets, D. F. C. M., Smits, A. P. T., Solleder, E., Inglin, B., Geile, B., Somssich, I., Schwarz, E., Speit, G., Mehnert, K., Vogel, W., Stahl, A., Hartung, M., Devictor, M., Guichaoua, M., Stoll, C., Roth, M.-P., Dott, B., Tabor, A., Madsen, M., Tommerup, N., Traut, W., Chavin-Colin, F., Junien, C., Vekemans, M., Esseltine, D., Venegas, W., Lasne, Cl, Chouroulinkov, I., Vidal, F., Navarro, J., Templado, C., Egozcue, J., Viegas-Péquignot, E., Malfoy, B., Taillandier, E., Leng, M., Viinikka, Y., Spielmann, H., Boldin, S., Volobouev, V. T., Webb, G. C., Krumins, E., Wegner, R.-D., Lüdtke, E.-L., Weith, A., Westerman, M., Thomson, R., Sinclair, A., Yacobi, Y. Z., Feldman, M., Yoon, J. S., Bennett, M. D., editor, Gropp, A., editor, and Wolf, U., editor

Published
1984
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8. Characterization of pKa Values and Titration Shifts in the Cytotoxic Ribonuclease α-Sarcin by NMR. Relationship between Electrostatic Interactions, Structure, and Catalytic Function

Author

Ramón Campos-Olivas, José Manuel Pérez-Cañadillas, Manuel Rico, Martínez del Pozo A, Marta Bruix, Jorge Santoro, José G. Gavilanes, Lacadena J, Dirección General de Investigación Científica y Técnica, DGICT (España), Dirección General de Enseñanza Superior e Investigación Científica (España), and Fundación Vicente Ferrer

Subjects
Models, Molecular, Titration curve, Macromolecular Substances, Stereochemistry, Static Electricity, Biochemistry, Catalysis, Fungal Proteins, Active center, chemistry.chemical_compound, Ribonuclease alpha, Endoribonucleases, Side chain, Histidine, Ribonuclease T1, Carboxylate, Nuclear Magnetic Resonance, Biomolecular, Cytotoxins, Titrimetry, Glutamic acid, Hydrogen-Ion Concentration, Guanine Nucleotides, Enzyme Activation, Aspergillus, chemistry, Titration, Protons
Abstract

The electrostatic behavior of titrating groups in α-sarcin was investigated using 1H NMR spectroscopy. A total of 209 chemical shift titration curves corresponding to different protons in the molecule were determined over the pH range of 3.0−8.5. Nonlinear least-squares fits of the data to simple relationships derived from the Henderson−Hasselbalch equation led to the unambiguous determination of pKa values for all glutamic acid and histidine residues, as well as for the C-terminal carboxylate and most of the aspartic acids in the free enzyme. The ionization constants of catalytically relevant histidines, His50 and His137, and glutamic acid, Glu96, in the α-sarcin−2‘-GMP complex were also determined. The pKa values of 15 ionizable groups (C-carboxylate, six aspartic acids, four glutamic acids, and four histidines) were found to be close to their normal values. On the other hand, a number of side chain groups, including those in the active center, showed pKa values far from their intrinsic values. Thus, the pKa values for active site residues His50, Glu96, and His137 were 7.7, 5.2, and 5.8 in the free enzyme and 7.6, ∼4.8, and 6.8 in the α-sarcin−2‘-GMP complex, respectively. The pKa values and the activity profile against ApA, as a function of pH, are in agreement with the proposed enzymatic mechanism (in common with RNase T1 and the family of the microbial ribonucleases), in which Glu96 and His137 act as a general base and general acid, respectively. In almost all microbial ribonucleases, a Phe−His interaction is present, which affects the pKa of one of the His residues at the active site (His137). The absence of this interaction in α-sarcin would explain the lower pKa value of this His residue, and provides an explanation for the decreased RNase activity of this protein as compared to those of other microbial ribonucleases., This work was supported by the Direccio´n General de Investigacio´n Cientı´fica y Te´cnica (Spain) (PB93-0189) and by the Direccio´n General de Ensen˜anza Superior (Spain) (PB96-0601). J.L. is a recipient of a fellowship from the Fundacio´n Ferrer (Barcelona).

Published
1998
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32. 1H and 15N nuclear magnetic resonance assignment and secondary structure of the cytotoxic ribonuclease alpha-Sarcin

Author

Campos-Olivas, R., Bruix, M., Santoro, J., Martínez del Pozo, A., Lacadena, J., Gavilanes, J. G., and Rico, M.

Subjects
Fungal Proteins, Aspergillus, Magnetic Resonance Spectroscopy, Nitrogen Isotopes, Cytotoxins, Endoribonucleases, Molecular Sequence Data, Amino Acid Sequence, Protons, Protein Structure, Secondary, Research Article
Abstract

The ribosome-inactivating protein alpha-Sarcin (alpha S) is a 150-residue fungal ribonuclease that, after entering sensitive cells, selectively cleaves a single phosphodiester bond in an universally conserved sequence of the major rRNA to inactivate the ribosome and thus exert its cytotoxic action. As a first step toward establishing the structure-dynamics-function relationships in this system, we have carried out the assignment of the 1H and 15N NMR spectrum of alpha S on the basis of homonuclear (1H-1H) and heteronuclear (1H-15N) two-dimensional correlation spectra of a uniformly 15N-labeled sample, and two selectively 15N-labeled (Tyr and Phe) samples, as well as a single three-dimensional experiment. The secondary structure of alpha S, as derived from the characteristic patterns of dipolar connectivities between backbone protons, conformational chemical shifts, and the protection of backbone amide protons against exchange, consists of a long N-terminal beta-hairpin, a short alpha-helical segment, and a C-terminal beta-sheet of five short strands arranged in a + 1, + 1, + 1, + 1 topology, connected by long loops in which the 13 Pro residues are located.

Published
1996

49. Nucleolus organizer competition in Triticum aestivum - Aegilops umbellulata chromosome addition lines.

Author

Lacadena, J. and Cermeño, M.

Abstract

The nucleolar organizer activity of wheat ( Triticum aestivum, AABBDD) and Aegilops umbellulata (UU) chromosomes have been analyzed in the complete set of the chromosome addition lines by using a highly reproducible silver-staining procedure. Chromosomes 1U and 5U produce the partial inactivation of wheat nucleolar organizer chromosomes 6B, 1B and 5D. The chromosomes D and G from Ae. umbellulata, which are not SAT-chromosomes, seem to specifically influence the activity of wheat NORs. The predominant status of the U genome with respect to nucleolar competition in the Triticeae is confirmed. [ABSTRACT FROM AUTHOR]

Published
1986
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50. The transmission of rye B chromosomes in natural pollination.

Author

Puertas, M. and Lacadena, J.

Abstract

This paper examines the transmission of B chromosomes in natural (but controlled) pollination, in order to obtain results which can be applied to natural populations of rye. The frequencies of the female gametes in both 2n= 14+1 and 2n=14+2 rye plants have been estimated with reference to their chromatid constitution. From the results obtained on the offspring, it seems that preferential distribution takes place during female meiosis of 2n= 14+2 plants. It has been demonstrated that pollen carrying B chromosomes formed in plants of 2n=14+2 was more competitive than normal pollen. On the contrary, when it was formed from plants 2n=14+1, B chromosome elimination by pollen was total. This process may be considered as sporophytic determination. The genetic significance of the presence of B chromosomes in natural populations is discussed. It is proposed that B chromosomes may be the cytological expression of a complex evolutionary system which results in conservation of population genetic variability. [ABSTRACT FROM AUTHOR]

Published
1975
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