Evidence map›Paper›PMID 25127513›Full record

ArticleMolecular cell2014

Lysine acetylation controls local protein conformation by influencing proline isomerization.

Françoise S Howe, Ivan Boubriak, Matthew J Sale, Anitha Nair, David Clynes, Anne Grijzenhout, Struan C Murray, Ronja Woloszczuk, Jane Mellor

Abstract read
In one paragraph

Article in Molecular cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. NJournal of proteome research · 2017
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. The interplay of post-translational modification and gene therapy.Drug design, development and therapy · 2016
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Françoise S HoweDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Ivan BoubriakDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Matthew J SaleDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Anitha NairDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
David ClynesDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Anne GrijzenhoutDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Struan C MurrayDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Ronja WoloszczukDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Jane MellorDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. Electronic address: jane.mellor@bioch.ox.ac.uk.

Funding

Medical Research Council G0900747 91070Wellcome TrustWellcome Trust 089156MAWellcome Trust 090532/Z/09/Z
6 · The paper itself

Abstract

Gene transcription responds to stress and metabolic signals to optimize growth and survival. Histone H3 (H3) lysine 4 trimethylation (K4me3) facilitates state changes, but how levels are coordinated with the environment is unclear. Here, we show that isomerization of H3 at the alanine 15-proline 16 (A15-P16) peptide bond is influenced by lysine 14 (K14) and controls gene-specific K4me3 by balancing the actions of Jhd2, the K4me3 demethylase, and Spp1, a subunit of the Set1 K4 methyltransferase complex. Acetylation at K14 favors the A15-P16trans conformation and reduces K4me3. Environmental stress-induced genes are most sensitive to the changes at K14 influencing H3 tail conformation and K4me3. By contrast, ribosomal protein genes maintain K4me3, required for their repression during stress, independently of Spp1, K14, and P16. Thus, the plasticity in control of K4me3, via signaling to K14 and isomerization at P16, informs distinct gene regulatory mechanisms and processes involving K4me3.

Indexed as

ChromatinEpigenesis, GeneticHistonesIsomerismLysineProlineProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStress, PhysiologicalChromatinHistonesLysineProlineSaccharomyces cerevisiae Proteins

Identifiers

PMID25127513
PMCPMC4157579

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.