J 2025

Assembly of the Xrn2/Rat1–Rai1–Rtt103 termination complexes in mesophilic and thermophilic organisms

DIKUNOVÁ, Alžbeta; Nikola NOSKOVÁ; Jan H. OVERBECK; Martin POLÁK; David STELZIG et. al.

Basic information

Original name

Assembly of the Xrn2/Rat1–Rai1–Rtt103 termination complexes in mesophilic and thermophilic organisms

Authors

DIKUNOVÁ, Alžbeta; Nikola NOSKOVÁ; Jan H. OVERBECK; Martin POLÁK; David STELZIG; David ZAPLETAL; Karel KUBÍČEK; Jiří NOVÁČEK; Remco SPRANGERS and Richard ŠTEFL

Edition

Structure, ENGLAND, CELL PRESS, 2025, 0969-2126

Other information

Language

English

Type of outcome

Article in a journal

Country of publisher

United States of America

Confidentiality degree

is not subject to a state or trade secret

References:

Organization

Středoevropský technologický institut – Repository – Repository

UT WoS

001424171800001

EID Scopus

2-s2.0-85215253831

Keywords in English

exoribonuclease Xrn2; Rat1; pomyerase RNAPII; CTD; Rtt103; structure

Links

EH22_008/0004575, research and development project. GA22-19896S, research and development project. CIISB II, large research infrastructures.
Changed: 13/3/2025 00:50, RNDr. Daniel Jakubík

Abstract

V originále

The 50–30 exoribonuclease Xrn2, known as Rat1 in yeasts, terminates mRNA transcription by RNA polymeraseII (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 a-helical fold. These different torpedo complex assemblies reflect adaptations to the environment and impact complex recruitment to RNAPII.

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