The target of the DEAH-box NTP triphosphatase Prp43 in Saccharomyces cerevisiae spliceosomes is the U2 snRNP-intron interaction
The DEAH-box NTPase Prp43 and its cofactors Ntr1 and Ntr2 form the NTR complex and are required for disassembling intron-lariat spliceosomes (ILS) and defective earlier spliceosomes. However, the Prp43 binding site in the spliceosome and its target(s) are unknown. We show that Prp43 fused to Ntr1�...
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eLife Sciences Publications Ltd
2016-04-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/15564 |
| _version_ | 1811180614562349056 |
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| author | Jean-Baptiste Fourmann Olexandr Dybkov Dmitry E Agafonov Marcel J Tauchert Henning Urlaub Ralf Ficner Patrizia Fabrizio Reinhard Lührmann |
| author_facet | Jean-Baptiste Fourmann Olexandr Dybkov Dmitry E Agafonov Marcel J Tauchert Henning Urlaub Ralf Ficner Patrizia Fabrizio Reinhard Lührmann |
| author_sort | Jean-Baptiste Fourmann |
| collection | DOAJ |
| description | The DEAH-box NTPase Prp43 and its cofactors Ntr1 and Ntr2 form the NTR complex and are required for disassembling intron-lariat spliceosomes (ILS) and defective earlier spliceosomes. However, the Prp43 binding site in the spliceosome and its target(s) are unknown. We show that Prp43 fused to Ntr1's G-patch motif (Prp43_Ntr1GP) is as efficient as the NTR in ILS disassembly, yielding identical dissociation products and recognizing its natural ILS target even in the absence of Ntr1’s C-terminal-domain (CTD) and Ntr2. Unlike the NTR, Prp43_Ntr1GP disassembles earlier spliceosomal complexes (A, B, Bact), indicating that Ntr2/Ntr1-CTD prevents NTR from disrupting properly assembled spliceosomes other than the ILS. The U2 snRNP-intron interaction is disrupted in all complexes by Prp43_Ntr1GP, and in the spliceosome contacts U2 proteins and the pre-mRNA, indicating that the U2 snRNP-intron interaction is Prp43’s major target. |
| first_indexed | 2024-04-11T09:06:14Z |
| format | Article |
| id | doaj.art-77ca72ef612c484b8264a63da2c7c456 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-11T09:06:14Z |
| publishDate | 2016-04-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-77ca72ef612c484b8264a63da2c7c4562022-12-22T04:32:37ZengeLife Sciences Publications LtdeLife2050-084X2016-04-01510.7554/eLife.15564The target of the DEAH-box NTP triphosphatase Prp43 in Saccharomyces cerevisiae spliceosomes is the U2 snRNP-intron interactionJean-Baptiste Fourmann0Olexandr Dybkov1Dmitry E Agafonov2Marcel J Tauchert3Henning Urlaub4Ralf Ficner5Patrizia Fabrizio6Reinhard Lührmann7https://orcid.org/0000-0002-6403-4432Department of Cellular Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, GermanyDepartment of Cellular Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, GermanyDepartment of Cellular Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, GermanyDepartment of Molecular Structure Biology, Institute for Microbiology and Genetics, Georg August University of Göttingen, Göttingen, GermanyBionalytics, Institute for Clinical Chemistry, University Medical Center Göttingen, Göttingen, Germany; Bioanalytical Mass Spectrometry Group, Max Planck Institute for Biophysical Chemistry, Göttingen, GermanyDepartment of Molecular Structure Biology, Institute for Microbiology and Genetics, Georg August University of Göttingen, Göttingen, GermanyDepartment of Cellular Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, GermanyDepartment of Cellular Biochemistry, Max-Planck-Institute for Biophysical Chemistry, Göttingen, GermanyThe DEAH-box NTPase Prp43 and its cofactors Ntr1 and Ntr2 form the NTR complex and are required for disassembling intron-lariat spliceosomes (ILS) and defective earlier spliceosomes. However, the Prp43 binding site in the spliceosome and its target(s) are unknown. We show that Prp43 fused to Ntr1's G-patch motif (Prp43_Ntr1GP) is as efficient as the NTR in ILS disassembly, yielding identical dissociation products and recognizing its natural ILS target even in the absence of Ntr1’s C-terminal-domain (CTD) and Ntr2. Unlike the NTR, Prp43_Ntr1GP disassembles earlier spliceosomal complexes (A, B, Bact), indicating that Ntr2/Ntr1-CTD prevents NTR from disrupting properly assembled spliceosomes other than the ILS. The U2 snRNP-intron interaction is disrupted in all complexes by Prp43_Ntr1GP, and in the spliceosome contacts U2 proteins and the pre-mRNA, indicating that the U2 snRNP-intron interaction is Prp43’s major target.https://elifesciences.org/articles/15564Humanspliceosomehelicases |
| spellingShingle | Jean-Baptiste Fourmann Olexandr Dybkov Dmitry E Agafonov Marcel J Tauchert Henning Urlaub Ralf Ficner Patrizia Fabrizio Reinhard Lührmann The target of the DEAH-box NTP triphosphatase Prp43 in Saccharomyces cerevisiae spliceosomes is the U2 snRNP-intron interaction eLife Human spliceosome helicases |
| title | The target of the DEAH-box NTP triphosphatase Prp43 in Saccharomyces cerevisiae spliceosomes is the U2 snRNP-intron interaction |
| title_full | The target of the DEAH-box NTP triphosphatase Prp43 in Saccharomyces cerevisiae spliceosomes is the U2 snRNP-intron interaction |
| title_fullStr | The target of the DEAH-box NTP triphosphatase Prp43 in Saccharomyces cerevisiae spliceosomes is the U2 snRNP-intron interaction |
| title_full_unstemmed | The target of the DEAH-box NTP triphosphatase Prp43 in Saccharomyces cerevisiae spliceosomes is the U2 snRNP-intron interaction |
| title_short | The target of the DEAH-box NTP triphosphatase Prp43 in Saccharomyces cerevisiae spliceosomes is the U2 snRNP-intron interaction |
| title_sort | target of the deah box ntp triphosphatase prp43 in saccharomyces cerevisiae spliceosomes is the u2 snrnp intron interaction |
| topic | Human spliceosome helicases |
| url | https://elifesciences.org/articles/15564 |
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