Evidence map›Paper›PMID 29670199›Full record

ArticleScientific reports2018

Evolutionary convergence and divergence in archaeal chromosomal proteins and Chromo-like domains from bacteria and eukaryotes.

Gurmeet Kaur, Lakshminarayan M Iyer, Srikrishna Subramanian, L Aravind

Abstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

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3 · Its place in the literature

Who cites it

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Refinement and curation of homologous groups facilitated by structure prediction.Protein science : a publication of the Protein Society · 2025
    Article
  4. On the evolutionary trail of MagRs.Zoological research · 2024
    Article
  5. Article
  6. Global Analysis of the WOX Transcription Factor Family inCurrent issues in molecular biology · 2023
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Archaea: The Final Frontier of Chromatin.Journal of molecular biology · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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.

Gurmeet KaurNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, 20894, USA.
Lakshminarayan M IyerNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, 20894, USA.
Srikrishna SubramanianBioinformatics Centre, CSIR-Institute of Microbial Technology, Sector 39A, Chandigarh, 160036, India. krishna@imtech.res.in.
L AravindNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, 20894, USA. aravind@mail.nih.gov.

Funding

Evolutionary Analysis and Comparative Genomics of Protein SuperfamiliesZIALM594244 · NLM · NATIONAL LIBRARY OF MEDICINE · PI ARAVIND, L · 2009 to 2025
$20.3M
6 · The paper itself

Abstract

SH3-fold-β-barrel domains of the chromo-like superfamily recognize epigenetic marks in eukaryotic proteins. Their provenance has been placed either in archaea, based on apparent structural similarity to chromatin-compacting Sul7d and Cren7 proteins, or in bacteria based on the presence of sequence homologs. Using sequence and structural evidence we establish that the archaeal Cren7/Sul7 proteins emerged from a zinc ribbon (ZnR) ancestor. Further, we show that the ancestral eukaryotic chromo-like domains evolved from bacterial versions, likely acquired from early endosymbioses, which already possessed an aromatic cage for recognition of modified amino-groups. These bacterial versions are part of a radiation of secreted SH3-fold domains, which spawned both chromo-like domains and classical SH3 domains in the context of peptide-recognition in the peptidoglycan or the extracellular matrix. This establishes that Cren7/Sul7 converged to a "SH3"-like state from a ZnR precursor via the loss of metal-chelation and acquisition of stronger hydrophobic interactions; it is unlikely to have participated in the evolution of the chromo-like domains. We show that archaea possess several Cren7/Sul7-related proteins with intact Zn-chelating ligands, which we predict to play previously unstudied roles in chromosome segregation during cell-division comparable to the PRC barrel and CdvA domain proteins.

Indexed as

Biological EvolutionProtein Interaction Domains and MotifsAmino Acid SequenceArchaeaBacteriaDNA-Binding ProteinsEukaryotaModels, MolecularProtein Conformationsrc Homology DomainsStructure-Activity RelationshipDNA-Binding Proteins

Identifiers

PMID29670199
PMCPMC5906684

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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.