Evidence map›Paper›PMID 22106294›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Displacement of the canonical single-stranded DNA-binding protein in the Thermoproteales.

Sonia Paytubi, Stephen A McMahon, Shirley Graham, Huanting Liu, Catherine H Botting, Kira S Makarova, Eugene V Koonin, James H Naismith, Malcolm F White

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. 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
1.7field-weighted citation impact, top 16% 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, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Single-Stranded DNA-Binding Proteins in the Archaea.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  6. Unlimited Cooperativity ofFrontiers in microbiology · 2021
    Article
  7. The Essential, Ubiquitous Single-Stranded DNA-Binding Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  8. Open biology · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Archaeology of eukaryotic DNA replication.Cold Spring Harbor perspectives in biology · 2013
    Review
  17. Article
  18. Article
  19. 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

9 authors at 2 institutions in 2 countries.

Sonia PaytubiBiomedical Sciences Research Complex, University of St Andrews, Fife KY16 9ST, United Kingdom.
Stephen A McMahon
Shirley Graham
Huanting Liu
Catherine H Botting
Kira S Makarova
Eugene V Koonin
James H Naismith
Malcolm F White
University of St Andrews · GBNational Institutes of Health · US

Funding

Finding Protein Sequence Motifs--Methods And ApplicationsZIALM000061 · NLM · NATIONAL LIBRARY OF MEDICINE · PI KOONIN, EUGENE V · 2009 to 2025
$10.6M
Biotechnology and Biological Sciences Research Council BBS/B/14426Biotechnology and Biological Sciences Research Council BB/S/B14450Wellcome Trust
6 · The paper itself

Abstract

ssDNA-binding proteins (SSBs) based on the oligonucleotide-binding fold are considered ubiquitous in nature and play a central role in many DNA transactions including replication, recombination, and repair. We demonstrate that the Thermoproteales, a clade of hyperthermophilic Crenarchaea, lack a canonical SSB. Instead, they encode a distinct ssDNA-binding protein that we term "ThermoDBP," exemplified by the protein Ttx1576 from Thermoproteus tenax. ThermoDBP binds specifically to ssDNA with low sequence specificity. The crystal structure of Ttx1576 reveals a unique fold and a mechanism for ssDNA binding, consisting of an extended cleft lined with hydrophobic phenylalanine residues and flanked by basic amino acids. Two ssDNA-binding domains are linked by a coiled-coil leucine zipper. ThermoDBP appears to have displaced the canonical SSB during the diversification of the Thermoproteales, a highly unusual example of the loss of a "ubiquitous" protein during evolution.

Indexed as

Cloning, MolecularCrystallography, X-RayDNA-Binding ProteinsProtein BindingProtein FoldingThermoprotealesDNA-Binding Proteins

Identifiers

PMID22106294
PMCPMC3289382
OpenAlexW2161394043

What OpenQuestion holds

Textmetadata
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.