Evidence map›Paper›PMID 17391511›Full record

ArticleBMC structural biology2007

On the origin of the histone fold.

Vikram Alva, Moritz Ammelburg, Johannes Söding, Andrei N Lupas

Abstract readComparative Study
In one paragraph

Article in BMC structural biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Review
  2. Article
  3. Multisubstrate specificity shaped the complex evolution of the aminotransferase family across the tree of life.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. The impact of solubility and electrostatics on fibril formation by the H3 and H4 histones.Protein science : a publication of the Protein Society · 2011
    Article
  19. Experimental evidence for the role of domain swapping in the evolution of the histone fold.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  20. The Histone Database: an integrated resource for histones and histone fold-containing proteins.Database : the journal of biological databases and curation · 2011
    Article
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.

Vikram AlvaDepartment of Protein Evolution, Max-Planck-Institute for Developmental Biology, Tübingen, Germany. vikram.alva@tuebingen.mpg.de <vikram.alva@tuebingen.mpg.de>
Moritz Ammelburg
Johannes Söding
Andrei N Lupas

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHistones organize the genomic DNA of eukaryotes into chromatin. The four core histone subunits consist of two consecutive helix-strand-helix motifs and are interleaved into heterodimers with a unique fold. We have searched for the evolutionary origin of this fold using sequence and structure comparisons, based on the hypothesis that folded proteins evolved by combination of an ancestral set of peptides, the antecedent domain segments.

resultsOur results suggest that an antecedent domain segment, corresponding to one helix-strand-helix motif, gave rise divergently to the N-terminal substrate recognition domain of Clp/Hsp100 proteins and to the helical part of the extended ATPase domain found in AAA+ proteins. The histone fold arose subsequently from the latter through a 3D domain-swapping event. To our knowledge, this is the first example of a genetically fixed 3D domain swap that led to the emergence of a protein family with novel properties, establishing domain swapping as a mechanism for protein evolution.

conclusionThe helix-strand-helix motif common to these three folds provides support for our theory of an 'ancient peptide world' by demonstrating how an ancestral fragment can give rise to 3 different folds.

Indexed as

Evolution, MolecularProtein FoldingStructural Homology, ProteinArchaeal ProteinsBacterial ProteinsDatabases, ProteinHistonesProtein Structure, TertiaryArchaeal ProteinsBacterial ProteinsHistones

Identifiers

PMID17391511
PMCPMC1847821

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.