Evidence map›Paper›PMID 29131864›Full record

ArticlePloS one2017

Comparison of histone-like HU protein DNA-binding properties and HU/IHF protein sequence alignment.

Dmitri Kamashev, Yulia Agapova, Sergey Rastorguev, Anna A Talyzina, Konstantin M Boyko, Dmitry A Korzhenevskiy, Anna Vlaskina, Raif Vasilov, Vladimir I Timofeev, Tatiana V Rakitina

Open access · goldAbstract readComparative Study
In one paragraph

Article in PloS one, 2017. 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
1.6field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Bacteriophage protein Gp46 is a cross-species inhibitor of nucleoid-associated HU proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Acetylation at Lysine 86 ofFrontiers in microbiology · 2021
    Article
  12. NontypeableBiofilm · 2020
    Article
  13. Article
  14. Article
  15. The structural basis of African swine fever virus pA104R binding to DNA and its inhibition by stilbene derivatives.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Urease Expression in PathogenicFrontiers in microbiology · 2020
    Article
  17. Transcription of Bacterial Chromatin.Journal of molecular biology · 2019
    Review
  18. Review
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

10 authors at 2 institutions in 1 country.

Dmitri KamashevKurchatov Complex of NBICS-Technologies, National Research Center «Kurchatov Institute», Moscow, Russian Federation.ORCID http://orcid.org/0000-0003-4158-5300
Yulia AgapovaKurchatov Complex of NBICS-Technologies, National Research Center «Kurchatov Institute», Moscow, Russian Federation.
Sergey RastorguevKurchatov Complex of NBICS-Technologies, National Research Center «Kurchatov Institute», Moscow, Russian Federation.
Anna A TalyzinaMoscow Institute of Physics and Technology, Dolgoprudny, Moscow Region, Russian Federation.
Konstantin M BoykoKurchatov Complex of NBICS-Technologies, National Research Center «Kurchatov Institute», Moscow, Russian Federation.
Dmitry A KorzhenevskiyKurchatov Complex of NBICS-Technologies, National Research Center «Kurchatov Institute», Moscow, Russian Federation.
Anna VlaskinaKurchatov Complex of NBICS-Technologies, National Research Center «Kurchatov Institute», Moscow, Russian Federation.
Raif VasilovKurchatov Complex of NBICS-Technologies, National Research Center «Kurchatov Institute», Moscow, Russian Federation.
Vladimir I TimofeevKurchatov Complex of NBICS-Technologies, National Research Center «Kurchatov Institute», Moscow, Russian Federation.
Tatiana V RakitinaKurchatov Complex of NBICS-Technologies, National Research Center «Kurchatov Institute», Moscow, Russian Federation.
Kurchatov Institute · RUMoscow Institute of Physics and Technology · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe structure and function of bacterial nucleoid are controlled by histone-like proteins of HU/IHF family, omnipresent in bacteria and also founding archaea and some eukaryotes.HU protein binds dsDNA without sequence specificity and avidly binds DNA structures with propensity to be inclined such as forks, three/four-way junctions, nicks, overhangs and DNA bulges. Sequence comparison of thousands of known histone-like proteins from diverse bacteria phyla reveals relation between HU/IHF sequence, DNA-binding properties and other protein features. METHODOLOGY AND PRINCIPAL

findingsPerformed alignment and clusterization of the protein sequences show that HU/IHF family proteins can be unambiguously divided into three groups, HU proteins, IHF_A and IHF_B proteins. HU proteins, IHF_A and IHF_B proteins are further partitioned into several clades for IHF and HU; such a subdivision is in good agreement with bacterial taxonomy. We also analyzed a hundred of 3D fold comparative models built for HU sequences from all revealed HU clades. It appears that HU fold remains similar in spite of the HU sequence variations. We studied DNA-binding properties of HU from N. gonorrhoeae, which sequence is similar to one of E.coli HU, and HU from M. gallisepticum and S. melliferum which sequences are distant from E.coli protein. We found that in respect to dsDNA binding, only S. melliferum HU essentially differs from E.coli HU. In respect to binding of distorted DNA structures, S. melliferum HU and E.coli HU have similar properties but essentially different from M. gallisepticum HU and N. gonorrhea HU. We found that in respect to dsDNA binding, only S. melliferum HU binds DNA in non-cooperative manner and both mycoplasma HU bend dsDNA stronger than E.coli and N. gonorrhoeae. In respect to binding to distorted DNA structures, each HU protein has its individual profile of affinities to various DNA-structures with the increased specificity to DNA junction. CONCLUSIONS AND SIGNIFICANCE: HU/IHF family proteins sequence alignment and classification are updated. Comparative modeling demonstrates that HU protein 3D folding's even more conservative than HU sequence. For the first time, DNA binding characteristics of HU from N. gonorrhoeae, M. gallisepticum and S. melliferum are studied. Here we provide detailed analysis of the similarity and variability of DNA-recognizing and bending of four HU proteins from closely and distantly related HU clades.

Indexed as

Sequence Homology, Amino AcidAmino Acid SequenceBacterial ProteinsBinding SitesDNA, BacterialDNA-Binding ProteinsHistonesModels, MolecularNucleic Acid ConformationBacterial ProteinsDNA, BacterialDNA-Binding Proteinshistone-like protein HU, bacteriaHistones

Identifiers

PMID29131864
PMCPMC5683647
OpenAlexW2769182010

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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.