Evidence map›Paper›PMID 31980943›Full record

ArticleExtremophiles : life under extreme conditions2020

Consensus protein engineering on the thermostable histone-like bacterial protein HUs significantly improves stability and DNA binding affinity.

Anastasios Georgoulis, Maria Louka, Stratos Mylonas, Philemon Stavros, George Nounesis, Constantinos E Vorgias

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Article in Extremophiles : life under extreme conditions, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Protein Stability: Enhancement and Measurement.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  2. Article
  3. Active site center redesign increases protein stability preserving catalysis in thioredoxin.Protein science : a publication of the Protein Society · 2022
    Article
  4. 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

6 authors at 2 institutions in 1 country.

Anastasios GeorgoulisDepartment of Biochemistry and Molecular Biology, National and Kapodistrian University of Athens, 157 01, Zografou, Greece.
Maria LoukaDepartment of Biochemistry and Molecular Biology, National and Kapodistrian University of Athens, 157 01, Zografou, Greece.
Stratos MylonasDepartment of Biochemistry and Molecular Biology, National and Kapodistrian University of Athens, 157 01, Zografou, Greece.
Philemon StavrosBiomolecular Physics Laboratory, INRASTES, National Centre for Scientific Research "Demokritos", 153 10, Agia Paraskevi, Greece.
George NounesisBiomolecular Physics Laboratory, INRASTES, National Centre for Scientific Research "Demokritos", 153 10, Agia Paraskevi, Greece.
Constantinos E VorgiasDepartment of Biochemistry and Molecular Biology, National and Kapodistrian University of Athens, 157 01, Zografou, Greece. cvorgias@biol.uoa.gr.
National and Kapodistrian University of Athens · GRNational Centre of Scientific Research "Demokritos" · GR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Consensus-based protein engineering strategy has been applied to various proteins and it can lead to the design of proteins with enhanced biological performance. Histone-like HUs comprise a protein family with sequence variety within a highly conserved 3D-fold. HU function includes compacting and regulating bacterial DNA in a wide range of biological conditions in bacteria. To explore the possible impact of consensus-based design in the thermodynamic stability of HU proteins, the approach was applied using a dataset of sequences derived from a group of 40 mesostable, thermostable, and hyperthermostable HUs. The consensus-derived HU protein was named HUBest, since it is expected to perform best. The synthetic HU gene was overexpressed in E. coli and the recombinant protein was purified. Subsequently, HUBest was characterized concerning its correct folding and thermodynamic stability, as well as its ability to interact with plasmid DNA. A substantial increase in HUBest stability at high temperatures is observed. HUBest has significantly improved biological performance at ambience temperature, presenting very low K

Indexed as

Protein EngineeringAmino Acid SequenceBacterial ProteinsConsensus SequenceDNA, BacterialEscherichia coliHistonesProtein BindingProtein StabilityBacterial ProteinsDNA, BacterialHistonesConsensus designDNA binding activityHU histone-like proteinThermostability

Identifiers

PMID31980943
OpenAlexW3003037462

What OpenQuestion holds

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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.