Evidence map›Paper›PMID 28452979›Full record

ArticleNature microbiology2017

Structural basis for λN-dependent processive transcription antitermination.

Nelly Said, Ferdinand Krupp, Ekaterina Anedchenko, Karine F Santos, Olexandr Dybkov, Yong-Heng Huang, Chung-Tien Lee, Bernhard Loll, Elmar Behrmann, Jörg Bürger and 6 more

Open access · bronzeAbstract read
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In one paragraph

Article in Nature microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.0field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

48 citing papers in PubMed, 71 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

16 authors at 6 institutions in 1 country.

Nelly SaidLaboratory of Structural Biochemistry, Freie Universität Berlin, Takustraβe 6, D-14195 Berlin, Germany.
Ferdinand KruppMedizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.
Ekaterina AnedchenkoLaboratory of Structural Biochemistry, Freie Universität Berlin, Takustraβe 6, D-14195 Berlin, Germany.
Karine F SantosLaboratory of Structural Biochemistry, Freie Universität Berlin, Takustraβe 6, D-14195 Berlin, Germany.
Olexandr DybkovDepartment of Cellular Biochemistry, Max Planck Institut für biophysikalische Chemie, Am Fassberg 11, D-37077 Göttingen, Germany.
Yong-Heng HuangLaboratory of Structural Biochemistry, Freie Universität Berlin, Takustraβe 6, D-14195 Berlin, Germany.
Chung-Tien LeeBioanalytical Mass Spectrometry, Max Planck Institut für biophysikalische Chemie, Am Fassberg 11, D-37077 Göttingen, Germany.
Bernhard LollLaboratory of Structural Biochemistry, Freie Universität Berlin, Takustraβe 6, D-14195 Berlin, Germany.ORCID http://orcid.org/0000-0001-7928-4488
Elmar BehrmannMedizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.
Jörg BürgerMedizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.
Thorsten MielkeInstitut für Klinische Chemie, Bioanalytik, Universitätsmedizin Göttingen, Robert-Koch-Straße 40, D-35075 Göttingen, Germany.
Justus LoerkeMedizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.
Henning UrlaubBioanalytical Mass Spectrometry, Max Planck Institut für biophysikalische Chemie, Am Fassberg 11, D-37077 Göttingen, Germany.
Christian M T SpahnMedizinische Physik und Biophysik, Charité - Universitätsmedizin Berlin, Charitéplatz 1, D-10117 Berlin, Germany.
Gert WeberLaboratory of Structural Biochemistry, Freie Universität Berlin, Takustraβe 6, D-14195 Berlin, Germany.
Markus C WahlLaboratory of Structural Biochemistry, Freie Universität Berlin, Takustraβe 6, D-14195 Berlin, Germany.ORCID http://orcid.org/0000-0002-2811-5307
Freie Universität Berlin · DECharité - Universitätsmedizin Berlin · DEUniversitätsmedizin Göttingen · DEHelmholtz-Zentrum Berlin für Materialien und Energie · DEMax Planck Institute for Biophysical Chemistry · DEMax Planck Institute for Molecular Genetics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

λN-mediated processive antitermination constitutes a paradigmatic transcription regulatory event, during which phage protein λN, host factors NusA, NusB, NusE and NusG, and an RNA nut site render elongating RNA polymerase termination-resistant. The structural basis of the process has so far remained elusive. Here we describe a crystal structure of a λN-NusA-NusB-NusE-nut site complex and an electron cryo-microscopic structure of a complete transcription antitermination complex, comprising RNA polymerase, DNA, nut site RNA, all Nus factors and λN, validated by crosslinking/mass spectrometry. Due to intrinsic disorder, λN can act as a multiprotein/RNA interaction hub, which, together with nut site RNA, arranges NusA, NusB and NusE into a triangular complex. This complex docks via the NusA N-terminal domain and the λN C-terminus next to the RNA exit channel on RNA polymerase. Based on the structures, comparative crosslinking analyses and structure-guided mutagenesis, we hypothesize that λN mounts a multipronged strategy to reprogram the transcriptional machinery, which may include (1) the λN C terminus clamping the RNA exit channel, thus stabilizing the DNA:RNA hybrid; (2) repositioning of NusA and RNAP elements, thus redirecting nascent RNA and sequestering the upstream branch of a terminator hairpin; and (3) hindering RNA engagement of termination factor ρ and/or obstructing ρ translocation on the transcript.

Indexed as

Terminator Regions, GeneticTranscription, GeneticBacterial ProteinsBinding SitesDNA-Directed RNA PolymerasesEscherichia coliEscherichia coli ProteinsGene Expression RegulationRho FactorRibosomal ProteinsRNARNA-Binding ProteinsTranscription Factorsantiterminator proteins, BacteriaBacterial ProteinsDNA-Directed RNA PolymerasesEscherichia coli ProteinsRho FactorRibosomal ProteinsRNARNA-Binding ProteinsTranscription Factors

Identifiers

PMID28452979
OpenAlexW2609081491

What OpenQuestion holds

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Registered trials

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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.