The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/00216208:11310/23:10474056

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2023

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biochemical Society Transactions

ISSN

0300-5127

e-ISSN

1470-8752

Svazek periodika

51

Číslo periodika v rámci svazku

1

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

11

Strana od-do

125-135

Kód UT WoS článku

001161371500003

EID výsledku v databázi Scopus

2-s2.0-85148759962