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18 documents found
1: Title: Structure of a human catalytic step I spliceosome.
Authors: Zhan, Xiechao, et.al. .
Journal: Science (New York, N.Y.) (Science), 2018 .
Snippet: The step I splicing factors CCDC49 and CCDC94 (Cwc25 and Yju2 in S. cerevisiae, respectively) closely interact with the DEAH-family ATPase/helicase Prp16 and bridge the gap between Prp16 and the active site RNA elements.
Affiliation: Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China. Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences and School of Medicine, Tsinghua University, Beijing 100084, China. yancy05@mails.tsinghua.edu.cn shi-lab@tsinghua.edu.cn. Technology Center for Protein Sciences, Ministry of Education Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China. Institute of Biology, Westlake Institute for Advanced Study, Westlake University, Shilongshan Road No. 18, Xihu District, Hangzhou 310064, Zhejiang Province, China. .
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2: Title: Structure of a spliceosome remodelled for exon ligation.
Authors: Fica, Sebastian M, et.al. .
Journal: Nature, Vol. 542 (7641): 377-380, 2017 .
Snippet: Recently reported structures of the spliceosomal C complex with the cleaved 5' exon and lariat-3'-exon bound to the catalytic centre revealed that branching-specific factors such as Cwc25 lock the branch helix into position for nucleophilic attack of the branch adenosine at the 5' splice site.
Affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK. .
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3: Title: A central role of Cwc25 in spliceosome dynamics during the catalytic phase of pre-mRNA splicing.
Authors: Tseng, Chi-Kang, et.al. .
Journal: RNA (New York, N.Y.) (Rna), Vol. 23 (4): 546-556, 2017 .
Snippet: Cwc25 binds tightly to the spliceosome after the reaction and is then removed from the spliceosome, which normally requires DExD/H-box protein Prp16 and ATP hydrolysis, to allow the occurrence of the second reaction.
Affiliation: Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan 115, Republic of China. .
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4: Title: Structure of a yeast step II catalytically activated spliceosome.
Authors: Yan, Chuangye, et.al. .
Journal: Science (New York, N.Y.) (Science), Vol. 355 (6321): 149-155, 2017 .
Snippet: The step I splicing factors Cwc25 and Yju2 have been dissociated from the active site.
Affiliation: Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China. Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China. shi-lab@tsinghua.edu.cn. .
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5: Title: Cryo-EM structure of the spliceosome immediately after branching.
Authors: Galej, Wojciech P, et.al. .
Journal: Nature, Vol. 537 (7619): 197-201, 2016 .
Snippet: Isy1 and the step-one factors Yju2 and Cwc25 stabilize docking of the branch helix.
Affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK. .
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6: Title: Structure of a yeast catalytic step I spliceosome at 3.4 Å resolution.
Authors: Wan, Ruixue, et.al. .
Journal: Science (New York, N.Y.) (Science), Vol. 353 (6302): 895-904, 2016 .
Snippet: Specific placement of these RNA elements at the catalytic cavity of Prp8 is stabilized by 15 protein components, including Snu114 and the splicing factors Cwc21, Cwc22, Cwc25, and Yju2.
Affiliation: Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China. Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China. shi-lab@tsinghua.edu.cn. .
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7: Title: Dynamic Contacts of U2, RES, Cwc25, Prp8 and Prp45 Proteins with the Pre-mRNA Branch-Site and 3' Splice Site during Catalytic Activation and Step 1 Catalysis in Yeast Spliceosomes.
Authors: Schneider, Cornelius, et.al. .
Journal: PLoS genetics (Plos Genet), Vol. 11 (9): e1005539, 2015 .
Snippet: Upon step 1 catalysis, Cwc25 contacts with the branch-site region, and enhanced crosslinks of Prp8 and Prp45 with nucleotides surrounding the branch-site were observed.
Affiliation: Max Planck Institute for Biophysical Chemistry, Department of Cellular Biochemistry, Göttingen, Germany. .
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8: Title: Remodeling of U2-U6 snRNA helix I during pre-mRNA splicing by Prp16 and the NineTeen Complex protein Cwc2.
Authors: Hogg, Rebecca, et.al. .
Journal: Nucleic acids research (Nucleic Acids Res), Vol. 42 (12): 8008-23, 2014 .
Snippet: The ATPase Prp16 remodels the spliceosome between the first and second steps of splicing by catalyzing release of first step factors Yju2 and Cwc25 as well as destabilizing U2-U6 snRNA helix I. How Prp16 destabilizes U2-U6 helix I is not clear.
Affiliation: Faculty of Life Sciences, The University of Manchester, Oxford Road, Manchester, M13 9PT. Faculty of Life Sciences, The University of Manchester, Oxford Road, Manchester, M13 9PT rokeefe@manchester.ac.uk. .
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9: Title: Biased Brownian ratcheting leads to pre-mRNA remodeling and capture prior to first-step splicing.
Authors: Krishnan, Ramya, et.al. .
Journal: Nature structural & molecular biology (Nat Struct Mol Biol), Vol. 20 (12): 1450-7, 2013 .
Snippet: Addition of Cwc25, a small heat-stable splicing factor, then strongly biases this equilibrium toward the proximal conformation, promoting efficient first-step splicing.
Affiliation: Department of Chemistry, Single Molecule Analysis Group, University of Michigan, Ann Arbor, Michigan, USA. .
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10: Title: Serum proteome changes following human immunodeficiency virus infection.
Authors: Haarburger, David, et.al. .
Journal: Clinical laboratory (Clin Lab), Vol. 59 (5-6): 639-46, 2013 .
Snippet: The proteins found to be increased were identified as pre-mRNA-splicing factor CWC25 homolog and 60S ribosomal protein L4.
Affiliation: Division of Chemical Pathology, National Health Laboratory Service, University of Cape Town, South Africa. david.haarburger@uct.ac.za .
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11: Title: Molecular dissection of step 2 catalysis of yeast pre-mRNA splicing investigated in a purified system.
Authors: Ohrt, Thomas, et.al. .
Journal: RNA (New York, N.Y.) (Rna), Vol. 19 (7): 902-15, 2013 .
Snippet: Spliceosome remodeling by Prp16 appears to be subtle as only the step 1 factor Cwc25 is dissociated prior to step 2 catalysis, with its release dependent on docking of the 3'SS to the active site and Prp16 action.
Affiliation: Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany. .
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12: Title: The spliceosome catalyzes debranching in competition with reverse of the first chemical reaction.
Authors: Tseng, Chi-Kang, et.al. .
Journal: RNA (New York, N.Y.) (Rna), Vol. 19 (7): 971-81, 2013 .
Snippet: The reactions are catalyzed by the spliceosome, a large ribonucleoprotein complex composed of five small nuclear RNAs and numerous protein factors.
Affiliation: Institute of Molecular Biology, Academia Sinica, Nankang, Taipei, Taiwan 11529, Republic of China. .
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13: Title: A weak spliceosome-binding domain of Yju2 functions in the first step and bypasses Prp16 in the second step of splicing.
Authors: Chiang, Ting-Wei, et.al. .
Journal: Molecular and cellular biology (Mol Cell Biol), Vol. 33 (9): 1746-55, 2013 .
Snippet: Prp16 is known to mediate destabilization of Yju2 and Cwc25 after the first reaction to allow progression of the second reaction.
Affiliation: Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan, Republic of China. .
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14: Title: Link of NTR-mediated spliceosome disassembly with DEAH-box ATPases Prp2, Prp16, and Prp22.
Authors: Chen, Hsin-Chou, et.al. .
Journal: Molecular and cellular biology (Mol Cell Biol), Vol. 33 (3): 514-25, 2013 .
Snippet: We found that NTR could catalyze the disassembly of affinity-purified spliceosomes arrested specifically after the ATP-dependent action of DEAH-box ATPase Prp2, Prp16, or Prp22 but not at steps before the action of these ATPases or upon their binding to the spliceosome.
Affiliation: Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, Taiwan. .
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15: Title: Prp2-mediated protein rearrangements at the catalytic core of the spliceosome as revealed by dcFCCS.
Authors: Ohrt, Thomas, et.al. .
Journal: RNA (New York, N.Y.) (Rna), Vol. 18 (6): 1244-56, 2012 .
Snippet: Conversely, high-affinity binding sites are created for Yju2 and Cwc25 during catalytic activation, consistent with their requirement for step 1 catalysis.
Affiliation: Max Planck Institute for Biophysical Chemistry, D-37077 Göttingen, Germany. .
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16: Title: DEAH-box ATPase Prp16 has dual roles in remodeling of the spliceosome in catalytic steps.
Authors: Tseng, Chi-Kang, et.al. .
Journal: RNA (New York, N.Y.) (Rna), Vol. 17 (1): 145-54, 2011 .
Snippet: The detailed mechanism of their action was not well understood until recently, when Prp2 was shown to be required for the release of U2 components SF3a and SF3b, presumably to allow the binding of Cwc25 to promote the first transesterification reaction.
Affiliation: Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, Taiwan 112, Republic of China. .
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17: Title: Reconstitution of both steps of Saccharomyces cerevisiae splicing with purified spliceosomal components.
Authors: Warkocki, Zbigniew, et.al. .
Journal: Nature structural & molecular biology (Nat Struct Mol Biol), Vol. 16 (12): 1237-43, 2009 .
Snippet: Spliceosomes stalled before step 1 of this process were purified to near-homogeneity from a temperature-sensitive mutant of the RNA helicase Prp2, compositionally defined, and shown to catalyze efficient step 1 when supplemented with recombinant Prp2, Spp2 and Cwc25, thereby demonstrating that Cwc25 has a previously unknown role in promoting step 1. Step 2 catalysis additionally required Prp16, Slu7, Prp18 and Prp22.
Affiliation: Department of Cellular Biochemistry, Max Planck Institute of Biophysical Chemistry, Göttingen, Germany. .
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18: Title: Cwc25 is a novel splicing factor required after Prp2 and Yju2 to facilitate the first catalytic reaction.
Authors: Chiu, Ying-Fang, et.al. .
Journal: Molecular and cellular biology (Mol Cell Biol), Vol. 29 (21): 5671-8, 2009 .
Snippet: The affinity-purified spliceosome formed in Cwc25-depleted extracts contained only pre-mRNA and could be chased into splicing intermediates upon the addition of recombinant Cwc25 in an ATP-independent manner, suggesting that Cwc25 functions in the final step of the first catalytic reaction after the action of Prp2.
Affiliation: Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan 115, Republic of China. .
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