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

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.

Základní údaje

Originální název

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

Autoři

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

Vydání

Structure, Cell Press, 2025, 0969-2126

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.300 v roce 2024

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1016/j.str.2024.11.010

UT WoS

001424171800001

EID Scopus

2-s2.0-85215253831

Klíčová slova anglicky

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

Štítky

14312020, 143160, CF CRYO, CF PROT, RNA4T

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 12. 3. 2025 13:28, Mgr. Marie Novosadová Šípková, DiS.

Anotace

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.

Návaznosti

EH22_008/0004575, projekt VaV

Název: RNA pro terapii

GA22-19896S, projekt VaV

Název: Strukturní podstata pro opětovné sestavení nukleosomu při přepisu genu zprostředkovaná proteinem Spt6

Investor: Grantová agentura ČR, Strukturní podstata pro opětovné sestavení nukleosomu při přepisu genu zrostředkovaná proteinem Spt6

90127, velká výzkumná infrastruktura

Název: CIISB II

Přiložené soubory

PIIS0969212624005008.pdf

Citovat

DIKUNOVÁ, Alžbeta; Nikola NOSKOVÁ; Jan H. OVERBECK; Martin POLÁK; David STELZIG; David ZAPLETAL; Karel KUBÍČEK; Jiří NOVÁČEK; Remco SPRANGERS a Richard ŠTEFL. Assembly of the Xrn2/Rat1–Rai1–Rtt103 termination complexes in mesophilic and thermophilic organisms. Structure. Cell Press, 2025, roč. 33, č. 2, s. 300-310. ISSN 0969-2126. Dostupné z: https://doi.org/10.1016/j.str.2024.11.010.

@article{2459638,
   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_number = {2},
   doi = {https://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 = {https://www.sciencedirect.com/science/article/pii/S0969212624005008?ref=pdf_download&fr=RR-2&rr=8f0ce12baef9f976},
   volume = {33},
   year = {2025}
}

TY  - JOUR
ID  - 2459638
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  - 09692126
KW  - exoribonuclease Xrn2
KW  - Rat1
KW  - pomyerase RNAPII
KW  - CTD
KW  - Rtt103
KW  - structure
UR  - https://www.sciencedirect.com/science/article/pii/S0969212624005008?ref=pdf_download&fr=RR-2&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 a Richard ŠTEFL. Assembly of the Xrn2/Rat1–Rai1–Rtt103 termination complexes in mesophilic and thermophilic organisms. \textit{Structure}. Cell Press, 2025, roč.~33, č.~2, s.~300-310. ISSN~0969-2126. Dostupné z: https://doi.org/10.1016/j.str.2024.11.010.

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