Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi

SF3b155 and p14 are essential components of spliceosome core that recognize the branch point adenosine, a critical step in splicing in eukaryotes. Trypanosomes are unusual since every transcribed gene is processed by trans-splicing instead of cis-splicing. Thus, the trans-spliceosome emerges as an i...

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Autor principal: Avila, M.L
Otros Autores: Bercovich, N., Westergaard, G., Levin, M.J, Vázquez, M.P
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2007
Acceso en línea:Registro en Scopus
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LEADER 09029caa a22010697a 4500
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005 20230518203552.0
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024 7 |2 scopus  |a 2-s2.0-35348959421 
024 7 |2 Molecular Sequence Numbers  |a GENBANK: AY294609, AY895171; 
024 7 |2 cas  |a alanine, 56-41-7, 6898-94-8; Phosphoproteins; Protozoan Proteins; RNA-Binding Proteins; Ribonucleoprotein, U2 Small Nuclear; SF3B1 protein, human; U2 small nuclear ribonucleoprotein p14 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a BBRCA 
100 1 |a Avila, M.L. 
245 1 0 |a Mapping of the protein-binding interface between splicing factors SF3b155 and p14 of Trypanosoma cruzi 
260 |c 2007 
270 1 0 |m Vázquez, M.P.; Departamento de Fisiología, Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Vta. de obligado 2490, Buenos Aires, Argentina; email: mvazquez@fbmc.fcen.uba.ar 
506 |2 openaire  |e Política editorial 
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504 |a Docampo, R., Sensitivity of parasites to free radical damage by antiparasitic drugs (1990) Chem. Biol. Interact., 73, pp. 1-27 
504 |a Liang, X.H., Haritan, A., Uliel, S., Michaeli, S., trans and cis splicing in trypanosomatids: mechanism, factors and regulation (2003) Eukaryot. Cell, 2, pp. 830-840 
504 |a Vázquez, M., Atorrasagasti, C., Bercovich, N., Volcovich, R., Levin, M.J., Unique features of the Trypanosoma cruzi U2AF35 splicing factor (2003) Mol. Biochem. Parasitol., 128, pp. 77-81 
504 |a Brosi, R., Hauri, H.P., Krämer, A., Separation of splicing factor SF3 into two components and purification of SF3a activity (1993) J. Bio. Chem., 268, pp. 17640-17646 
504 |a Cass, D.M., Berglund, J.A., The SF3b155 N-terminal domain is a scaffold important for splicing (2006) Biochemistry, 45, pp. 10092-10101 
504 |a Golas, M.M., Sander, B., Will, C.L., Lührmann, R., Stark, H., Molecular architecture of the multiprotein splicing Factor SF3b (2003) Science, 300, pp. 980-984 
504 |a Will, C.L., Schneider, C., MacMillan, A.M., Katopodis, N.F., Neubauer, G., Will, M., Lührmann, R., Query, C.C., A novel U2 and U11/U12 snRNP protein that associates with the pre-mRNA branch site (2001) EMBO J., 20, pp. 4536-4546 
504 |a Spadaccini, R., Reist, U., Dybkov, O., Will, C., Frank, R., Stier, G., Corsini, L., Sattler, M., Biochemical and NMR analyses of an SF3b155-p14-U2AF-RNA interaction network involved in branch point definition during pre-mRNA splicing (2006) RNA, 12, pp. 410-425 
504 |a Schellenberg, M.J., Edwards, R.A., Ritchie, D.B., Kent, O.A., Golas, M.M., Stark, H., Lührmann, R., MacMillan, A.M., Crystal structure of core spliceosomal protein interface (2006) Proc. Natl. Acad. Sci. USA, 103, pp. 1266-1271 
504 |a Horton, R.M., PCR-mediated recombination and mutagenesis SOEing together tailor-made genes (1995) Mol. Biotechnol., 3, pp. 93-99 
504 |a Caro, F., Bercovich, N., Atorrasagasti, C., Levin, M.J., Vázquez, M.P., Protein interactions within the TcZFP zinc finger family members of Trypanosoma cruzi: implications for their functions (2005) Biochem. Biophys. Res. Commun., 333, pp. 1017-1025 
504 |a Reed, R., Initial splice site recognition and pairing during pre-mRNA splicing (1996) Curr. Opin. Genet. Dev., 6, pp. 215-220 
504 |a Eilbracht, J., Schmidt-Zachmann, M.S., Identification of a sequence element directing a protein to nuclear speckles (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 3849-3854 
504 |a Thickman, K.R., Swenson, M.C., Kabogo, J.M., Gryczynski, Z., Kielkopf, C.L., Multiple U2AF65 Binding Sites within SF3b155: thermodynamic and spectroscopic characterization of protein-protein interactions among pre-mRNA Splicing Factors (2006) J. Mol. Biol., 356, pp. 664-683 
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504 |a Kaida, D., Motoyoshi, H., Tashiro, E., Nojima, T., Hagiwara, M., Ishigami, K., Watanabe, H., Yoshida, M., Spliceostatin A targets SF3b and inhibits both splicing and nuclear retention of pre-mRNA (2007) Nat. Chem. Biol., 3, pp. 576-583 
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520 3 |a SF3b155 and p14 are essential components of spliceosome core that recognize the branch point adenosine, a critical step in splicing in eukaryotes. Trypanosomes are unusual since every transcribed gene is processed by trans-splicing instead of cis-splicing. Thus, the trans-spliceosome emerges as an interesting anti-parasitic drug target since this process is not present in mammalian hosts. Here, we present the orthologues of these proteins in Trypanosoma cruzi that interact strongly with each other. To define similarities and differences with the human pair, we performed a detailed alanine scan analysis that allowed us to identify the regions and the critical amino acids of T. cruzi SF3b155 involved in interaction with p14. We demonstrate that the T. cruzi SF3b155 interface is larger and contains more complex elements than its human counterpart. Additionally, our results provide the first insights into the core of the putative mRNA processing complex of trypanosomes. © 2007 Elsevier Inc. All rights reserved.  |l eng 
536 |a Detalles de la financiación: Fondo para la Investigación Científica y Tecnológica 
536 |a Detalles de la financiación: We thank Catalina Atorrasagasti for helpful discussions and assistance during the initial steps of the work presented in this paper. This work was supported by grants from FONCYT—PICT REDES 2003-00300, UBACyT X-153 (University of Buenos Aires) and PIP-CONICET 5492 to M.V. and WHO/TDR, South-South initiative (SSI-WHO/TDR) to M.J.L. M.V. and M.J.L. are members of the career of scientific investigator of CONICET, Argentina. MJL is a IIF Marie Curie fellow, EU project 040402-SMMAD. Appendix A 
593 |a Departamento de Fisiología, Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Vta. de obligado 2490, Buenos Aires, Argentina 
593 |a Institut Cochin, INSERM U567, Paris, France 
690 1 0 |a DRUG TARGETS 
690 1 0 |a PROTEIN INTERACTION 
690 1 0 |a TRANS-SPLICING 
690 1 0 |a ALANINE 
690 1 0 |a MESSENGER RNA 
690 1 0 |a PROTEIN DERIVATIVE 
690 1 0 |a PROTEIN P14 
690 1 0 |a SF3B155 PROTEIN 
690 1 0 |a UNCLASSIFIED DRUG 
690 1 0 |a ARTICLE 
690 1 0 |a DNA SPLICING 
690 1 0 |a GENE MAPPING 
690 1 0 |a NONHUMAN 
690 1 0 |a PRIORITY JOURNAL 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a PROTEIN PROCESSING 
690 1 0 |a SPLICEOSOME 
690 1 0 |a TRYPANOSOMA 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a AMINO ACID SEQUENCE 
690 1 0 |a ANIMALS 
690 1 0 |a HUMANS 
690 1 0 |a MOLECULAR SEQUENCE DATA 
690 1 0 |a NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR 
690 1 0 |a PHOSPHOPROTEINS 
690 1 0 |a PROTEIN BINDING 
690 1 0 |a PROTEIN STRUCTURE, TERTIARY 
690 1 0 |a PROTOZOAN PROTEINS 
690 1 0 |a RIBONUCLEOPROTEIN, U2 SMALL NUCLEAR 
690 1 0 |a RNA-BINDING PROTEINS 
690 1 0 |a SPLICEOSOMES 
690 1 0 |a TRYPANOSOMA CRUZI 
690 1 0 |a EUKARYOTA 
690 1 0 |a MAMMALIA 
690 1 0 |a TRYPANOSOMA CRUZI 
700 1 |a Bercovich, N. 
700 1 |a Westergaard, G. 
700 1 |a Levin, M.J. 
700 1 |a Vázquez, M.P. 
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