RNA Polymerase II CTD Tyrosine 1 Is Required for Efficient Termination by the Nrd1-Nab3-Sen1 Pathway.
Binding Sites
DNA Helicases
/ genetics
Gene Expression Regulation, Fungal
Mutation
Nuclear Proteins
/ genetics
Phosphorylation
Protein Binding
RNA Helicases
/ genetics
RNA Polymerase II
/ genetics
RNA-Binding Proteins
/ genetics
Saccharomyces cerevisiae
/ enzymology
Saccharomyces cerevisiae Proteins
/ genetics
Signal Transduction
Time Factors
Transcription Termination, Genetic
Tyrosine
CTD
Nab3
Nrd1
Pcf11
Pol II
Rtt103
Sen1
pausing
transcription termination
tyrosine 1
Journal
Molecular cell
ISSN: 1097-4164
Titre abrégé: Mol Cell
Pays: United States
ID NLM: 9802571
Informations de publication
Date de publication:
21 02 2019
21 02 2019
Historique:
received:
31
05
2018
revised:
09
09
2018
accepted:
29
11
2018
pubmed:
15
1
2019
medline:
25
6
2019
entrez:
15
1
2019
Statut:
ppublish
Résumé
In Saccharomyces cerevisiae, transcription termination at protein-coding genes is coupled to the cleavage of the nascent transcript, whereas most non-coding RNA transcription relies on a cleavage-independent termination pathway involving Nrd1, Nab3, and Sen1 (NNS). Termination involves RNA polymerase II CTD phosphorylation, but a systematic analysis of the contribution of individual residues would improve our understanding of the role of the CTD in this process. Here we investigated the effect of mutating phosphorylation sites in the CTD on termination. We observed widespread termination defects at protein-coding genes in mutants for Ser2 or Thr4 but rare defects in Tyr1 mutants for this genes class. Instead, mutating Tyr1 led to widespread termination defects at non-coding genes terminating via NNS. Finally, we showed that Tyr1 is important for pausing in the 5' end of genes and that slowing down transcription suppresses termination defects. Our work highlights the importance of Tyr1-mediated pausing in NNS-dependent termination.
Identifiants
pubmed: 30639244
pii: S1097-2765(18)31032-3
doi: 10.1016/j.molcel.2018.12.002
pii:
doi:
Substances chimiques
NAB3 protein, S cerevisiae
0
NRD1 protein, S cerevisiae
0
Nuclear Proteins
0
RNA-Binding Proteins
0
Saccharomyces cerevisiae Proteins
0
Tyrosine
42HK56048U
RNA Polymerase II
EC 2.7.7.-
SEN1 protein, S cerevisiae
EC 3.6.1.-
DNA Helicases
EC 3.6.4.-
RNA Helicases
EC 3.6.4.13
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
655-669.e7Subventions
Organisme : CIHR
ID : MOP-133 648
Pays : Canada
Informations de copyright
Copyright © 2018 Elsevier Inc. All rights reserved.