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

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

Přehled o publikaci

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:

URL URL URL

Organization

Středoevropský technologický institut – Repository – Repository

DOI

http://dx.doi.org/10.1016/j.str.2024.11.010

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.

Files attached

https://is.muni.cz/publication/2459638/PIIS0969212624005008.pdf

Cite

DIKUNOVÁ, Alžbeta, Nikola NOSKOVÁ, Jan H. OVERBECK, Martin POLÁK, David STELZIG, David ZAPLETAL, Karel KUBÍČEK, Jiří NOVÁČEK, Remco SPRANGERS and Richard ŠTEFL. Assembly of the Xrn2/Rat1–Rai1–Rtt103 termination complexes in mesophilic and thermophilic organisms. Structure. ENGLAND: CELL PRESS, 2025, vol. 33, No 2, p. 300-310. ISSN 0969-2126. Available from: https://dx.doi.org/10.1016/j.str.2024.11.010.

@article{68948,
   author = {Dikunová, Alžbeta and Nosková, Nikola and Overbeck, Jan H. and Polák, Martin and Stelzig, David and Zapletal, David and Kubíček, Karel and Nováček, Jiří and Sprangers, Remco and Štefl, Richard},
   article_location = {ENGLAND},
   article_number = {2},
   doi = {http://dx.doi.org/10.1016/j.str.2024.11.010},
   keywords = {exoribonuclease Xrn2; Rat1; pomyerase RNAPII; CTD; Rtt103; structure},
   language = {eng},
   issn = {0969-2126},
   journal = {Structure},
   title = {Assembly of the Xrn2/Rat1–Rai1–Rtt103 termination complexes in mesophilic and thermophilic organisms},
   url = {rr=8f0ce12baef9f976},
   volume = {33},
   year = {2025}
}

TY  - JOUR
ID  - 68948
AU  - Dikunová, Alžbeta - Nosková, Nikola - Overbeck, Jan H. - Polák, Martin - Stelzig, David - Zapletal, David - Kubíček, Karel - Nováček, Jiří - Sprangers, Remco - Štefl, Richard
PY  - 2025
TI  - Assembly of the Xrn2/Rat1–Rai1–Rtt103 termination complexes in mesophilic and thermophilic organisms
JF  - Structure
VL  - 33
IS  - 2
SP  - 300-310
EP  - 300-310
PB  - CELL PRESS
SN  - 0969-2126
KW  - exoribonuclease Xrn2
KW  - Rat1
KW  - pomyerase RNAPII
KW  - CTD
KW  - Rtt103
KW  - structure
UR  - rr=8f0ce12baef9f976
N2  - 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.
ER  -

DIKUNOVÁ, Alžbeta, Nikola NOSKOVÁ, Jan H. OVERBECK, Martin POLÁK, David STELZIG, David ZAPLETAL, Karel KUBÍČEK, Jiří NOVÁČEK, Remco SPRANGERS and Richard ŠTEFL. Assembly of the Xrn2/Rat1–Rai1–Rtt103 termination complexes in mesophilic and thermophilic organisms. \textit{Structure}. ENGLAND: CELL PRESS, 2025, vol.~33, No~2, p.~300-310. ISSN~0969-2126. Available from: https://dx.doi.org/10.1016/j.str.2024.11.010.