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  • 1
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    Molecular biology. RNP remodeling with DExH/D boxes (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Will, C L -- Luhrmann, R -- New York, N.Y. -- Science. 2001 Mar 9;291(5510):1916-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry Department, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany. cwill1@gwdg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11245200" target="_blank"〉PubMed〈/a〉
    Keywords: Acid Anhydride Hydrolases/*metabolism ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; DEAD-box RNA Helicases ; Fungal Proteins/metabolism ; Kinetics ; Nucleoside-Triphosphatase ; RNA Nucleotidyltransferases/metabolism ; RNA Precursors/metabolism ; RNA, Double-Stranded/*metabolism ; RNA, Small Nuclear/*metabolism ; *RNA-Binding Proteins ; Ribonucleoprotein, U1 Small Nuclear/*metabolism ; Ribonucleoproteins/metabolism ; Ribonucleoproteins, Small Nuclear/*metabolism ; Saccharomyces cerevisiae/genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Spliceosomes/*metabolism ; Vaccinia virus/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Identification of both shared and distinct proteins in the major and minor spliceosomes (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-06-18
    Description: In metazoans, two distinct spliceosomes catalyzing pre-messenger RNA splicing have been identified. Here, the human U11/U12 small nuclear ribonucleoprotein (snRNP), a subunit of the minor (U12-dependent) spliceosome, was isolated. Twenty U11/U12 proteins were identified, including subsets unique to the minor spliceosome or common to both spliceosomes. Common proteins include four U2 snRNP polypeptides that constitute the essential splicing factor SF3b. A 35-kilodalton U11-associated protein homologous to the U1 snRNP 70K protein was also identified. These data provide fundamental information about proteins of the minor spliceosome and shed light on its evolutionary relationship to the major spliceosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Will, C L -- Schneider, C -- Reed, R -- Luhrmann, R -- New York, N.Y. -- Science. 1999 Jun 18;284(5422):2003-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Molekularbiologie und Tumorforschung, Philipps-Universitat, 35037 Marburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10373121" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chromatography, Affinity ; Evolution, Molecular ; HeLa Cells ; Humans ; Introns ; Molecular Sequence Data ; Molecular Weight ; RNA Splicing ; Ribonucleoprotein, U1 Small Nuclear/*analysis/isolation & purification ; Ribonucleoprotein, U2 Small Nuclear/*analysis/isolation & purification ; Ribonucleoproteins, Small Nuclear/*analysis/isolation & purification ; Spliceosomes/*chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-02
    Description: Major structural changes occur in the spliceosome during its activation just before catalyzing the splicing of pre-messenger RNAs (pre-mRNAs). Whereas changes in small nuclear RNA (snRNA) conformation are well documented, little is known about remodeling of small nuclear ribonucleoprotein (snRNP) structures during spliceosome activation. Here, human 45S activated spliceosomes and a previously unknown 35S U5 snRNP were isolated by immunoaffinity selection and were characterized by mass spectrometry. Comparison of their protein components with those of other snRNP and spliceosomal complexes revealed a major change in protein composition during spliceosome activation. Our data also suggest that the U5 snRNP is dramatically remodeled at this stage, with the Prp19 complex and other factors tightly associating, possibly in exchange for other U5 proteins, and suggest that after catalysis the remodeled U5 is eventually released from the postsplicing complex as a 35S snRNP particle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Makarov, Evgeny M -- Makarova, Olga V -- Urlaub, Henning -- Gentzel, Marc -- Will, Cindy L -- Wilm, Matthias -- Luhrmann, Reinhard -- New York, N.Y. -- Science. 2002 Dec 13;298(5601):2205-8. Epub 2002 Oct 31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular Biochemistry, Max Planck Institute of Biophysical Chemistry, D-37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12411573" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Centrifugation, Density Gradient ; Humans ; Macromolecular Substances ; Mass Spectrometry ; Models, Genetic ; Nuclear Proteins/immunology/metabolism ; Nuclear Receptor Coactivators ; Precipitin Tests ; RNA Precursors/metabolism ; *RNA Splicing ; RNA, Small Nuclear/metabolism ; Ribonucleoprotein, U5 Small Nuclear/*chemistry/isolation & ; purification/metabolism ; Spliceosomes/chemistry/*metabolism ; Transcription Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Isolation of an active step I spliceosome and composition of its RNP core (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-03-07
    Description: Formation of catalytically active RNA structures within the spliceosome requires the assistance of proteins. However, little is known about the number and nature of proteins needed to establish and maintain the spliceosome's active site. Here we affinity-purified human spliceosomal C complexes and show that they catalyse exon ligation in the absence of added factors. Comparisons of the composition of the precatalytic versus the catalytic spliceosome revealed a marked exchange of proteins during the transition from the B to the C complex, with apparent stabilization of Prp19-CDC5 complex proteins and destabilization of SF3a/b proteins. Disruption of purified C complexes led to the isolation of a salt-stable ribonucleoprotein (RNP) core that contained both splicing intermediates and U2, U5 and U6 small nuclear RNA plus predominantly U5 and human Prp19-CDC5 proteins and Prp19-related factors. Our data provide insights into the spliceosome's catalytic RNP domain and indicate a central role for the aforementioned proteins in sustaining its catalytically active structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bessonov, Sergey -- Anokhina, Maria -- Will, Cindy L -- Urlaub, Henning -- Luhrmann, Reinhard -- England -- Nature. 2008 Apr 17;452(7189):846-50. doi: 10.1038/nature06842. Epub 2008 Mar 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular Biochemistry, Max Planck Institute of Biophysical Chemistry, D-37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18322460" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Catalytic Domain ; Exons/genetics ; Humans ; Multiprotein Complexes/*chemistry/genetics/*isolation & purification ; RNA Splice Sites/genetics ; RNA Splicing ; RNA, Messenger/genetics/metabolism ; RNA, Small Nuclear/analysis/chemistry/genetics/isolation & purification ; Ribonucleoproteins/*analysis/*chemistry/genetics/isolation & purification ; Spliceosomes/*chemistry/*genetics
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 5
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    HSPC117 is the essential subunit of a human tRNA splicing ligase complex (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-02-12
    Description: Splicing of mammalian precursor transfer RNA (tRNA) molecules involves two enzymatic steps. First, intron removal by the tRNA splicing endonuclease generates separate 5' and 3' exons. In animals, the second step predominantly entails direct exon ligation by an elusive RNA ligase. Using activity-guided purification of tRNA ligase from HeLa cell extracts, we identified HSPC117, a member of the UPF0027 (RtcB) family, as the essential subunit of a tRNA ligase complex. RNA interference-mediated depletion of HSPC117 inhibited maturation of intron-containing pre-tRNA both in vitro and in living cells. The high sequence conservation of HSPC117/RtcB proteins is suggestive of RNA ligase roles of this protein family in various organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Popow, Johannes -- Englert, Markus -- Weitzer, Stefan -- Schleiffer, Alexander -- Mierzwa, Beata -- Mechtler, Karl -- Trowitzsch, Simon -- Will, Cindy L -- Luhrmann, Reinhard -- Soll, Dieter -- Martinez, Javier -- New York, N.Y. -- Science. 2011 Feb 11;331(6018):760-4. doi: 10.1126/science.1197847.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), A-1030 Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21311021" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Exons ; HeLa Cells ; Humans ; Introns ; Molecular Sequence Data ; Proteins/*chemistry/isolation & purification/*metabolism ; RNA Interference ; RNA Ligase (ATP)/*chemistry/isolation & purification/*metabolism ; RNA Precursors/*metabolism ; *RNA Splicing ; RNA, Transfer/*metabolism ; Spliceosomes/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Molecular architecture of the multiprotein splicing factor SF3b (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-05-10
    Description: The splicing factor SF3b is a multiprotein complex essential for the accurate excision of introns from pre-messenger RNA. As an integral component of the U2 small nuclear ribonucleoprotein (snRNP) and the U11/U12 di-snRNP, SF3b is involved in the recognition of the pre-messenger RNA's branch site within the major and minor spliceosomes. We have determined the three-dimensional structure of the human SF3b complex by single-particle electron cryomicroscopy at a resolution of less than 10 angstroms, allowing identification of protein domains with known structural folds. The best fit of a modeled RNA-recognition motif indicates that the protein p14 is located in the central cavity of the complex. The 22 tandem helical repeats of the protein SF3b155 are located in the outer shell of the complex enclosing p14.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Golas, Monika M -- Sander, Bjoern -- Will, Cindy L -- Luhrmann, Reinhard -- Stark, Holger -- New York, N.Y. -- Science. 2003 May 9;300(5621):980-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12738865" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Cryoelectron Microscopy ; HeLa Cells ; Humans ; Image Processing, Computer-Assisted ; Macromolecular Substances ; Models, Molecular ; Multiprotein Complexes ; Phosphoproteins/*chemistry ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA Precursors/chemistry/metabolism ; RNA Splicing ; *RNA-Binding Proteins ; Repetitive Sequences, Amino Acid ; Ribonucleoprotein, U2 Small Nuclear/*chemistry ; Spliceosomes/chemistry/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Through the glass lightly (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Luhrmann, R -- Will, C L -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1616-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17808161" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 8
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    Inhibition of RNA helicase Brr2 by the C-terminal tail of the spliceosomal protein Prp8 (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-05-25
    Description: The Ski2-like RNA helicase Brr2 is a core component of the spliceosome that must be tightly regulated to ensure correct timing of spliceosome activation. Little is known about mechanisms of regulation of Ski2-like helicases by protein cofactors. Here we show by crystal structure and biochemical analyses that the Prp8 protein, a major regulator of the spliceosome, can insert its C-terminal tail into Brr2's RNA-binding tunnel, thereby intermittently blocking Brr2's RNA-binding, adenosine triphosphatase, and U4/U6 unwinding activities. Inefficient Brr2 repression is the only recognizable phenotype associated with certain retinitis pigmentosa-linked Prp8 mutations that map to its C-terminal tail. Our data show how a Ski2-like RNA helicase can be reversibly inhibited by a protein cofactor that directly competes with RNA substrate binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mozaffari-Jovin, Sina -- Wandersleben, Traudy -- Santos, Karine F -- Will, Cindy L -- Luhrmann, Reinhard -- Wahl, Markus C -- New York, N.Y. -- Science. 2013 Jul 5;341(6141):80-4. doi: 10.1126/science.1237515. Epub 2013 May 23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23704370" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; *Binding, Competitive ; Carrier Proteins/genetics/*metabolism ; Humans ; Molecular Sequence Data ; Mutation ; Protein Structure, Tertiary ; RNA/*metabolism ; RNA Helicases/metabolism ; RNA-Binding Proteins ; Ribonucleoprotein, U4-U6 Small Nuclear/metabolism ; Ribonucleoprotein, U5 Small Nuclear/metabolism ; Ribonucleoproteins, Small Nuclear/*antagonists & inhibitors/chemistry/*metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Spliceosomes/*metabolism ; Substrate Specificity
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 9
    Electronic Resource
    Electronic Resource
    Protein composition of mammalian spliceosomal snRNPs (1993)
    Springer
    Molecular biology reports 18 (1993), S. 121-126 
    Details
    ISSN: 1573-4978
    Keywords: snRNP proteins ; pre-mRNA splicing ; snRNPs
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00986766
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    Paper (German National Licenses)
    Fulltext
  • 10
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    Protein composition of human prespliceosomes isolated by a tobramycin affinity-selection method (2002)
    National Academy of Sciences
    Details
    Publication Date: 2002-12-11
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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