Evidence map›Paper›PMID 28180347›Full record

ArticleNucleic acids research2017

Biochemical characterization of the helicase Sen1 provides new insights into the mechanisms of non-coding transcription termination.

Zhong Han, Domenico Libri, Odil Porrua

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Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

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40citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

40 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

3 authors.

Zhong HanInstitut Jacques Monod, UMR7592, Centre Nationale pour la Recherche Scientifique (CNRS), Université Paris-Diderot, Sorbonne Paris Cité, F-75205 Paris, France.
Domenico LibriInstitut Jacques Monod, UMR7592, Centre Nationale pour la Recherche Scientifique (CNRS), Université Paris-Diderot, Sorbonne Paris Cité, F-75205 Paris, France.
Odil PorruaInstitut Jacques Monod, UMR7592, Centre Nationale pour la Recherche Scientifique (CNRS), Université Paris-Diderot, Sorbonne Paris Cité, F-75205 Paris, France.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pervasive transcription is widespread and needs to be controlled in order to avoid interference with gene expression. In Saccharomyces cerevisiae, the highly conserved helicase Sen1 plays a key role in restricting pervasive transcription by eliciting early termination of non-coding transcription. However, many aspects of the mechanism of termination remain unclear. In this study we characterize the biochemical activities of Sen1 and their role in termination. First, we demonstrate that the helicase domain (HD) is sufficient to dissociate the elongation complex (EC) in vitro. Both full-length Sen1 and its HD can translocate along single-stranded RNA and DNA in the 5΄ to 3΄ direction. Surprisingly, however, we show that Sen1 is a relatively poorly processive enzyme, implying that it must be recruited in close proximity to the RNA polymerase II (RNAPII) for efficient termination. We present evidence that Sen1 can promote forward translocation of stalled polymerases by acting on the nascent transcript. In addition, we find that dissociation of the EC by Sen1 is favoured by the reannealing of the DNA upstream of RNAPII. Taken together, our results provide new clues to understand the mechanism of Sen1-dependent transcription termination and a rationale for the kinetic competition between elongation and termination.

Indexed as

Transcription Termination, GeneticDNA HelicasesDNA, Single-StrandedModels, BiologicalNuclear ProteinsProtein DomainsRNA-Binding ProteinsRNA, FungalRNA HelicasesRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA HelicasesDNA, Single-StrandedNAB3 protein, S cerevisiaeNRD1 protein, S cerevisiaeNuclear ProteinsRNA-Binding ProteinsRNA, FungalRNA HelicasesRNA Polymerase IISaccharomyces cerevisiae ProteinsSEN1 protein, S cerevisiae

Identifiers

PMID28180347
PMCPMC5388409

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.