Evidence map›Paper›PMID 27693057›Full record

ArticleCell chemical biology2016

Analysis of the RNA Binding Specificity Landscape of C5 Protein Reveals Structure and Sequence Preferences that Direct RNase P Specificity.

Hsuan-Chun Lin, Jing Zhao, Courtney N Niland, Brandon Tran, Eckhard Jankowsky, Michael E Harris

Open access · bronzeAbstract read
In one paragraph

Article in Cell chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Suppression of theRNA (New York, N.Y.) · 2024
    Article
  5. RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Approaches for measuring the dynamics of RNA-protein interactions.Wiley interdisciplinary reviews. RNA · 2020
    Review
  14. Blind tests of RNA-protein binding affinity prediction.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Article
  17. Rules of RNA specificity of hnRNP A1 revealed by global and quantitative analysis of its affinity distribution.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Article
  19. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Hsuan-Chun LinDepartment of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Jing ZhaoDepartment of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Courtney N NilandDepartment of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Brandon TranDepartment of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Eckhard JankowskyDepartment of Biochemistry, Center for RNA Molecular Biology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
Michael E HarrisDepartment of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA. Electronic address: meh2@cwru.edu.
University School · US

Funding

GRADUATE TRAINING IN CELLULAR AND MOLECULAR BIOLOGYT32GM008056 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI DIEHL, JOHN ALAN, SNIDER, MARTIN D · 1985 to 2019
$7.1M
STRUCTURE/FUNCTION OF RIBONUCLEASE PR01GM056740 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI HARRIS, MICHAEL E. · 1998 to 2015
$4.8M
Enzymes and enzyme complexes in RNA metabolismR35GM118088 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI JANKOWSKY, ECKHARD · 2016 to 2022
$4.3M
Mechansim of DExH/D proteinsR01GM067700 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI JANKOWSKY, ECKHARD · 2003 to 2015
$4.2M
NIGMS NIH HHS R01 GM056740NIGMS NIH HHS R01 GM067700NIGMS NIH HHS R35 GM118088NIGMS NIH HHS T32 GM008056
6 · The paper itself

Abstract

RNA binding proteins (RBPs) are typically involved in non-equilibrium cellular processes, and specificity can arise from differences in ground state, transition state, or product states of the binding reactions for alternative RNAs. Here, we use high-throughput methods to measure and analyze the RNA association kinetics and equilibrium binding affinity for all possible sequence combinations in the precursor tRNA binding site of C5, the essential protein subunit of Escherichia coli RNase P. The results show that the RNA sequence specificity of C5 arises due to favorable RNA-protein interactions that stabilize the transition state for association and bound enzyme-substrate complex. Specificity is further impacted by unfavorable RNA structure involving the C5 binding site in the ground state. The results illustrate a comprehensive quantitative approach for analysis of RNA binding specificity, and show how both RNA structure and sequence preferences of an essential protein subunit direct the specificity of a ribonucleoprotein enzyme.

Indexed as

Base SequenceBinding SitesEscherichia coliEscherichia coli ProteinsModels, MolecularProtein ConformationRibonuclease PRNA, BacterialRNA PrecursorsEscherichia coli ProteinsRibonuclease Pribonuclease P, E coliRNA, BacterialRNA Precursorsenzyme kineticsribonuclease, tRNARNA binding proteinRNA specificity

Identifiers

PMID27693057
PMCPMC5088717
OpenAlexW2525407732

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

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.