Dikunova, Alzbeta and Noskova, Nikola and Overbeck, Jan H. and Polak, Martin and Stelzig, David and Zapletal, David and Kubicek, Karel and Novacek, Jiri and Sprangers, Remco and Stefl, Richard (2025) Assembly of the Xrn2/Rat1-Rai1-Rtt103 termination complexes in mesophilic and thermophilic organisms. STRUCTURE, 33 (2). pp. 300-310. ISSN 0969-2126, 1878-4186
Full text not available from this repository. (Request a copy)Abstract
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 b-sheet, while in the thermophile Rtt103 binds to a C-terminal helix of Rai1 via its CTD-interacting domain with an cc-helical fold. These different torpedo complex assemblies reflect adaptations to the environment and impact complex recruitment to RNAPII.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | RNA-POLYMERASE-II; PROMOTES TRANSCRIPTION TERMINATION; STRUCTURE VALIDATION; THERMAL-STABILITY; PROTEIN; MOLPROBITY; MECHANISM; DOMAIN; PHOSPHORYLATION; RAT1 |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Remco Sprangers |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 12 Aug 2026 04:12 |
| Last Modified: | 12 Aug 2026 04:12 |
| URI: | https://pred.uni-regensburg.de/id/eprint/67009 |
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