Structure and phase separation of the C-terminal domain of RNA polymerase II

The repetitive heptads in the C-terminal domain (CTD) of RPB1, the largest subunit of RNA Polymerase II (Pol II), play a critical role in the regulation of Pol II-based transcription. Recent findings on the structure of the CTD in the pre-initiation complex determined by cryo-EM and the novel phase...

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Published inBiological chemistry Vol. 404; no. 8; pp. 839 - 844
Main Authors Lushpinskaia, Irina P., Flores-Solis, David, Zweckstetter, Markus
Format Journal Article
LanguageEnglish
Published Germany De Gruyter 26.07.2023
Walter de Gruyter GmbH
Subjects
CTD
DNA-directed RNA polymerase
Ewings sarcoma
Gene regulation
Initiation complex
Kinases
liquid–liquid phase separation
Peptides
Phase separation
Phosphorylation
Proteins
RNA Pol II
RNA polymerase
RNA polymerase II
Spatial distribution
Temporal distribution
Transcription
Yeast
CTD
RNA Pol II
transcription
liquid–liquid phase separation
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Summary:The repetitive heptads in the C-terminal domain (CTD) of RPB1, the largest subunit of RNA Polymerase II (Pol II), play a critical role in the regulation of Pol II-based transcription. Recent findings on the structure of the CTD in the pre-initiation complex determined by cryo-EM and the novel phase separation properties of key transcription components offers an expanded mechanistic interpretation of the spatiotemporal distribution of Pol II during transcription. Current experimental evidence further suggests an exquisite balance between CTD’s local structure and an array of multivalent interactions that drive phase separation of Pol II and thus shape its transcriptional activity.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
ISSN:1431-6730
1437-4315
DOI:10.1515/hsz-2023-0136