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

0569154 - ÚOCHB 2024 RIV GB eng J - Článek v odborném periodiku
Cermakova, K. - Veverka, Václav - Hodges, H. C.
The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder.
Biochemical Society Transactions. Roč. 51, č. 1 (2023), s. 125-135. ISSN 0300-5127. E-ISSN 1470-8752
Grant CEP: GA ČR(CZ) GA22-03028S; GA MŠMT(CZ) EF16_019/0000729
Institucionální podpora: RVO:61388963
Klíčová slova: intrinsically disordered proteins * molecular scaffolds * structural biology * transcription
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 3.9, rok: 2022
Způsob publikování: Open access
https://doi.org/10.1042/BST20220342

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.
Trvalý link: https://hdl.handle.net/11104/0340490