Evidence map›Paper›PMID 28468956›Full record

ArticleEMBO reports2017

Structural insight into recognition of phosphorylated threonine-4 of RNA polymerase II C-terminal domain by Rtt103p.

Olga Jasnovidova, Magdalena Krejcikova, Karel Kubicek, Richard Stefl

Abstract read
In one paragraph

Article in EMBO reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

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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

4 authors.

Olga JasnovidovaCEITEC - Central European Institute of Technology, Masaryk University, Brno, Czech Republic olga.jasnovidova@ceitec.muni.cz richard.stefl@ceitec.muni.cz.ORCID 0000-0002-8362-7647
Magdalena KrejcikovaCEITEC - Central European Institute of Technology, Masaryk University, Brno, Czech Republic.
Karel KubicekCEITEC - Central European Institute of Technology, Masaryk University, Brno, Czech Republic.
Richard SteflCEITEC - Central European Institute of Technology, Masaryk University, Brno, Czech Republic olga.jasnovidova@ceitec.muni.cz richard.stefl@ceitec.muni.cz.ORCID 0000-0003-0558-5952

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation patterns of the C-terminal domain (CTD) of largest subunit of RNA polymerase II (called the CTD code) orchestrate the recruitment of RNA processing and transcription factors. Recent studies showed that not only serines and tyrosines but also threonines of the CTD can be phosphorylated with a number of functional consequences, including the interaction with yeast transcription termination factor, Rtt103p. Here, we report the solution structure of the Rtt103p CTD-interacting domain (CID) bound to Thr4 phosphorylated CTD, a poorly understood letter of the CTD code. The structure reveals a direct recognition of the phospho-Thr4 mark by Rtt103p CID and extensive interactions involving residues from three repeats of the CTD heptad. Intriguingly, Rtt103p's CID binds equally well Thr4 and Ser2 phosphorylated CTD A doubly phosphorylated CTD at Ser2 and Thr4 diminishes its binding affinity due to electrostatic repulsion. Our structural data suggest that the recruitment of a CID-containing CTD-binding factor may be coded by more than one letter of the CTD code.

Indexed as

PhosphorylationProtein BindingProtein KinasesProtein Structure, TertiaryProteolysisRNA Polymerase IISaccharomyces cerevisiae ProteinsSerineThreonineTranscription FactorsTranscription, GeneticTyrosineProtein KinasesRNA Polymerase IIRtt103 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSerineThreonineTranscription FactorsTyrosineNMRRNAPII CTD codeRNA processingstructural biology

Identifiers

PMID28468956
PMCPMC5452035

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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.