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.Základní údaje
Originální název
Termination of non-coding transcription in yeast relies on both an RNA Pol II CTD interaction domain and a CTD-mimicking region in Sen1
Autoři
HAN, Z.; Olga JASNOVIDOVA; N. HAIDARA; A. TUDEK; Karel KUBÍČEK ORCID; D. LIBRI; Richard ŠTEFL a O. PORRUA
Vydání
EMBO Journal, Hoboken (USA), WILEY-BLACKWELL, 2020, 0261-4189
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10608 Biochemistry and molecular biology
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 11.598
Kód RIV
RIV/00216224:14740/20:00114181
Organizační jednotka
Středoevropský technologický institut
UT WoS
000516807800001
EID Scopus
2-s2.0-85080149490
Klíčová slova anglicky
non-coding transcription; pervasive transcription; RNA polymerase II CTD; Sen1 helicase; transcription termination
Štítky
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 11. 3. 2021 18:50, Mgr. Pavla Foltynová, Ph.D.
Anotace
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.
Návaznosti
| GA18-11397S, projekt VaV |
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| LQ1601, projekt VaV |
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| 649030, interní kód MU |
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