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-Structure paper
| タイトル | Assembly of the Xrn2/Rat1-Rai1-Rtt103 termination complexes in mesophilic and thermophilic organisms. |
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| ジャーナル・号・ページ | Structure, Vol. 33, Issue 2, Page 300-310.e6, Year 2025 |
| 掲載日 | 2025年2月6日 |
著者 | Alzbeta Dikunova / Nikola Noskova / Jan H Overbeck / Martin Polak / David Stelzig / David Zapletal / Karel Kubicek / Jiri Novacek / Remco Sprangers / Richard Stefl / ![]() |
| PubMed 要旨 | The 5'-3' exoribonuclease Xrn2, known as Rat1 in yeasts, terminates mRNA transcription by RNA polymerase II (RNAPII). In the torpedo model of termination, the activity of Xrn2/Rat1 is enhanced by ...The 5'-3' exoribonuclease Xrn2, known as Rat1 in yeasts, terminates mRNA transcription by RNA polymerase II (RNAPII). In the torpedo model of termination, the activity of Xrn2/Rat1 is enhanced by Rai1, which is recruited to the termination site by Rtt103, an adaptor protein binding to the RNAPII C-terminal domain (CTD). The overall architecture of the Xrn2/Rat1-Rai1-Rtt103 complex remains unknown. We combined structural biology methods to characterize the torpedo complex from Saccharomyces cerevisiae and Chaetomium thermophilum. Comparison of the structures from these organisms revealed a conserved protein core fold of the subunits, but significant variability in their interaction interfaces. We found that in the mesophile, Rtt103 utilizes an unstructured region to augment a Rai1 β-sheet, while in the thermophile Rtt103 binds to a C-terminal helix of Rai1 via its CTD-interacting domain with an α-helical fold. These different torpedo complex assemblies reflect adaptations to the environment and impact complex recruitment to RNAPII. |
リンク | Structure / PubMed:39657659 |
| 手法 | EM (単粒子) |
| 解像度 | 2.65 - 3.28 Å |
| 構造データ | EMDB-18199, PDB-8q6v: EMDB-50048, PDB-9exs: EMDB-50566, PDB-9fms: |
| 化合物 | ![]() ChemComp-MG: |
| 由来 |
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キーワード | RNA BINDING PROTEIN / Rai1 nuclease / Rtt103 binding / structured / RNA binding |
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thermochaetoides thermophila (菌類)
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