Assembly of the Xrn2/Rat1-Rai1-Rtt103 termination complexes in mesophilic and thermophilic organisms
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F25%3A00617464" target="_blank" >RIV/68378050:_____/25:00617464 - isvavai.cz</a>
Alternative codes found
RIV/00216224:14740/25:00140423
Result on the web
<a href="https://doi.org/10.1016/j.str.2024.11.010" target="_blank" >https://doi.org/10.1016/j.str.2024.11.010</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.str.2024.11.010" target="_blank" >10.1016/j.str.2024.11.010</a>
Alternative languages
Result language
angličtina
Original language name
Assembly of the Xrn2/Rat1-Rai1-Rtt103 termination complexes in mesophilic and thermophilic organisms
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Structure
ISSN
0969-2126
e-ISSN
1878-4186
Volume of the periodical
33
Issue of the periodical within the volume
2
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
"300"-"310.e6"
UT code for WoS article
001424171800001
EID of the result in the Scopus database
2-s2.0-85215253831