The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00569154" target="_blank" >RIV/61388963:_____/23:00569154 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/23:10474056
Result on the web
<a href="https://doi.org/10.1042/BST20220342" target="_blank" >https://doi.org/10.1042/BST20220342</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1042/BST20220342" target="_blank" >10.1042/BST20220342</a>
Alternative languages
Result language
angličtina
Original language name
The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder
Original language description
Interaction scaffolds that selectively recognize disordered protein strongly shape protein interactomes. An important scaffold of this type that contributes to transcription is the TFIIS N-terminal domain (TND). The TND is a five-helical bundle that has no known enzym-atic activity, but instead selectively reads intrinsically disordered sequences of other proteins. Here, we review the structural and functional properties of TNDs and their cognate disordered ligands known as TND-interacting motifs (TIMs). TNDs or TIMs are found in prominent members of the transcription machinery, including TFIIS, super elongation complex, SWI/SNF, Mediator, IWS1, SPT6, PP1-PNUTS phosphatase, elongin, H3K36me3 readers, the transcription factor MYC, and others. We also review how the TND interac-tome contributes to the regulation of transcription. Because the TND is the most signifi-cantly enriched fold among transcription elongation regulators, TND-and TIM-driven interactions have widespread roles in the regulation of many transcriptional processes.
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
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biochemical Society Transactions
ISSN
0300-5127
e-ISSN
1470-8752
Volume of the periodical
51
Issue of the periodical within the volume
1
Country of publishing house
GB - UNITED KINGDOM
Number of pages
11
Pages from-to
125-135
UT code for WoS article
001161371500003
EID of the result in the Scopus database
2-s2.0-85148759962