Analysis of pre-mRNA and pre-rRNA processing factor Snu13p structure and mutants

Biochemical and Biophysical Research Communications

Volumn 360, Issue 4, 2007, Pages 857-862

  Dobbyn, Helen C ^a   McEwan, Paul A ^a   Krause, Andre ^b   Novak Frazer, Lily ^b   Bella, Jordi ^b   O'Keefe, Raymond T ^b  

^a UNIVERSITY OF NOTTINGHAM   (United Kingdom)

^b UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Crystal structure; Pre mRNA splicing; snoRNP; snRNP; Snu13p

Indexed keywords

GENE PRODUCT; MESSENGER RNA; RIBONUCLEOPROTEIN; RIBOSOME RNA; SMALL NUCLEAR RNA; SNU13P PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL ANALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; GENE STRUCTURE; GENETIC ANALYSIS; HUMAN; MUTANT; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN INTERACTION; RNA BINDING; TEMPERATURE SENSITIVE MUTANT; WILD TYPE;

CLONING, MOLECULAR; MODELS, MOLECULAR; MUTATION; RIBONUCLEOPROTEINS, SMALL NUCLEAR; RNA PRECURSORS; RNA, MESSENGER; RNA, RIBOSOMAL; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

SACCHAROMYCES CEREVISIAE;

EID: 34447579888     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.06.163     Document Type: Article

References (26)

1. Moore M.J., Query C.C., and Sharp P.A. Splicing of precursors to mRNA by the spliceosome. In: Gesteland R.F., and Atkins J.F. (Eds). The RNA World (1993), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York 303-357
2. Gottschalk A., Neubauer G., Banroques J., Mann M., Lührmann R., and Fabrizio P. Identification by mass spectrometry and functional analysis of novel proteins of the yeast [U4/U6.U5] tri-snRNP. EMBO J. 18 (1999) 4535-4548
3. Kuhn J.F., Tran E.J., and Maxwell E.S. Archael ribosomal protein L7 is a functional homologue of the eukaryotic 15.5K/Snu13p snoRNP core protein. Nucleic Acids Res. 30 (2002) 931-941
4. Stevens S.W., and Abelson J. Purification of the yeast U4/U6.U5 small nuclear ribonucleoprotein particle and identification of its proteins. Proc. Natl Acad. Sci. USA 96 (1999) 7226-7231
5. Watkins N.J., Ségault V., Charpentier B., Nottrott S., Fabrizio P., Bachi A., Wilm M., Rosbash M., Branlant C., and Lührmann R. A common core RNP structure shared between the small nucleolar box C/D RNPs and the spliceosomal U4 snRNP. Cell 103 (2000) 457-466
6. Granneman S., Pruijn G.J.M., Horstman W., van Venrooij W.J., Lührmann R., and Watkins N.J. The hU3-55K protein requires 15.5K binding to the box B/C motif as well as flanking RNA elements for its association with the U3 small nucleolar RNA in vitro. J. Biol. Chem. 277 (2002) 48490-48500
7. Nottrott S., Urlaub H., and Lührmann R. Hierarchical, clustered protein interactions with U4/U6 snRNA: a biochemical role for U4/U6 proteins. EMBO J. 21 (2002) 5527-5538
8. Reichow S.L., Hamma T., Ferre-D'Amare A.R., and Varani G. The structure and function of small nucleolar ribonucleoproteins. Nucleic Acids Res. 35 (2007) 1452-1464
9. Watkins N.J., Dickmanns A., and Lührmann R. Conserved stem II of the box C/D motif is essential for nucleolar localization and is required, along with the 15.5K protein, for the hierarchical assembly of the box C/D snoRNP. Mol. Cell Biol. 22 (2002) 8342-8352
10. Anthony J.G., Weidenhammer E.M., and Woolford J.L.J. The yeast prp3 protein is a U4/U6 snRNP protein necessary for integrity of the U4/U6 snRNP and the U4/U6.U5 tri-snRNP. RNA 3 (1997) 1143-1152
11. Banroques J., and Abelson J.N. PRP4: a protein of the yeast U4/U6 small nuclear ribonucleoprotein particle. Mol. Cell Biol. 9 (1989) 3710-3719
12. Peterson-Bjorn S.P., Soltyk A., Beggs J.D., and Friesen J.D. PRP4 (RNA4) from Saccharaomyces cerevisiae is associated with the U4/U6 small nuclear ribonucleoprotein particle. Mol. Cell Biol. 9 (1989) 3698-3709
13. Weidenhammer E.M., Ruiz-Noriega M., and Woolford J.L.J. Prp31p promotes the association of the U4/U6.U5 tri-snRNP with prespliceosomes to form spliceosomes in Saccharomyces cerevisiae. Mol. Cell Biol. 17 (1997) 3580-3588
14. Vidovic I., Nottrott S., Hartmuth K., Lührmann R., and Ficner R. Crystal structure of the spliceosomal 15.5 kDa protein bound to a U4 snRNA fragment. Mol. Cell 6 (2000) 1331-1342
15. Liu S., Li P., Dybkov O., Nottrott S., Hartmuth K., Lührmann R., Carlomagno T., and Wahl M.C. Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP. Science 316 (2007) 115-120
16. Oruganti S., Zhang Y., and Li H. Structural comparison of yeast snoRNP and spliceosomal protein Snu13p with its homologs. Biochem. Biophys. Res. Commun. 333 (2005) 550-554
17. Dobbyn H.C., and O'Keefe R.T. Analysis of Snu13p mutations reveals differential interactions with the U4 snRNA and U3 snoRNA. RNA 10 (2004) 308-320
18. The CCP4 suite: programs for protein crystallography, Acta Crystallogr. sect. D 50 (1994) 760-763.
19. Navaza J. Implementation of molecular replacement in AMoRe. Acta Crystallogr. Sect. D 57 (2001) 1367-1372
20. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., and Warren G.L. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. Sect. D 54 (1998) 905-921
21. McRee D. Practical Protein Crystallography. second ed. (1999), Academic press
22. Mao H., and Williamson J.R. Local folding coupled to RNA binding in the yeast ribosomal protein L30. J. Mol. Biol. 292 (1999) 345-359
23. Schultz A., Nottrott S., Watkins N.J., and Lührmann R. Protein-protein and protein-RNA contacts both contribute to the 15.5K-mediated assembly of the U4/U6 snRNP and the box C/D snoRNPs. Mol. Cell Biol. 26 (2006) 5146-5154
24. Ayadi L., Callebaut I., Saguez C., Villa T., Mornon J.P., and Banroques J. Functional and structural characterization of the prp3 binding domain of the yeast prp4 splicing factor. J. Mol. Biol. 284 (1998) 673-687
25. Chakshusmathi G., Mondal K., Lakshmi G.S., Singh G., Roy A., Ch R.B., Madhusudhanan S., and Varadarajan R. Design of temperature-sensitive mutants solely from amino acid sequence. Proc. Natl. Acad. Sci. USA 101 (2004) 7925-7930
26. Kapust R.B., and Waugh D.S. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8 (1999) 1668-1674