J
2020
Termination of non-coding transcription in yeast relies on both an RNA Pol II CTD interaction domain and a CTD-mimicking region in Sen1
HAN, Z., Olga JASNOVIDOVA, N. HAIDARA, A. TUDEK, Karel KUBÍČEK et. al.
Basic information
Original name
Termination of non-coding transcription in yeast relies on both an RNA Pol II CTD interaction domain and a CTD-mimicking region in Sen1
Authors
HAN, Z., Olga JASNOVIDOVA, N. HAIDARA, A. TUDEK, Karel KUBÍČEK, D. LIBRI, Richard ŠTEFL and O. PORRUA
Edition
EMBO Journal, Hoboken (USA), WILEY-BLACKWELL, 2020, 0261-4189
Other information
Type of outcome
Článek v odborném periodiku
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
Organization
Středoevropský technologický institut – Repository – Repository
Keywords in English
non-coding transcription; pervasive transcription; RNA polymerase II CTD; Sen1 helicase; transcription termination
Links
GA18-11397S, research and development project. LQ1601, research and development project. 649030, interní kód Repo.
V originále
Pervasive transcription is a widespread phenomenon leading to the production of a plethora of non-coding RNAs (ncRNAs) without apparent function. Pervasive transcription poses a threat to proper gene expression that needs to be controlled. In yeast, the highly conserved helicase Sen1 restricts pervasive transcription by inducing termination of non-coding transcription. However, the mechanisms underlying the specific function of Sen1 at ncRNAs are poorly understood. Here, we identify a motif in an intrinsically disordered region of Sen1 that mimics the phosphorylated carboxy-terminal domain (CTD) of RNA polymerase II, and structurally characterize its recognition by the CTD-interacting domain of Nrd1, an RNA-binding protein that binds specific sequences in ncRNAs. In addition, we show that Sen1-dependent termination strictly requires CTD recognition by the N-terminal domain of Sen1. We provide evidence that the Sen1-CTD interaction does not promote initial Sen1 recruitment, but rather enhances Sen1 capacity to induce the release of paused RNAPII from the DNA. Our results shed light on the network of protein-protein interactions that control termination of non-coding transcription by Sen1.
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