Evidence map›Paper›PMID 34272975›Full record

ArticleCurrent microbiology2021

Effect of lon Protease Overexpression on Endotoxin Production and Stress Resistance in Bacillus thuringiensis.

Mouktar Abdi Barkad, Aslı Bayraktar, Tugrul Doruk, Sedef Tunca

Abstract read
PubMed Publisher
In one paragraph

Article in Current microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

7 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Lon protease reprograms cellular physiology ofFrontiers in microbiology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. 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

4 authors at 2 institutions in 1 country.

Mouktar Abdi BarkadFaculty of Science, Molecular Biology and Genetics Department, Gebze Technical University, Gebze, 41400, Izmit, Turkey.ORCID http://orcid.org/0000-0002-1765-9536
Aslı BayraktarFaculty of Science, Molecular Biology and Genetics Department, Gebze Technical University, Gebze, 41400, Izmit, Turkey.ORCID http://orcid.org/0000-0001-7066-2112
Tugrul DorukFaculty of Art and Science, Molecular Biology and Genetics Department, Ondokuz Mayıs University, Atakum, 55200, Samsun, Turkey.ORCID http://orcid.org/0000-0002-0057-320X
Sedef TuncaFaculty of Science, Molecular Biology and Genetics Department, Gebze Technical University, Gebze, 41400, Izmit, Turkey. sgedik@gtu.edu.tr.ORCID http://orcid.org/0000-0001-6896-4904
Gebze Technical University · TROndokuz Mayıs University · TR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lon protease, an intracellular protease, plays a key role in cell homeostasis in bacteria and is involved in numerous physiological processes. In this work, we aimed to study the impact of Lon on the production of endotoxins and stress response in Bacillus thuringiensis, which is an important bioinsecticide alternative for toxic chemicals. For this purpose, lon gene was cloned into a multi-copy vector with its original promoter and transcriptional terminator and expressed in B. thuringiensis serovar israelensis ATCC 35,646. Our results showed that the recombinant lon gene transcribed and translated efficiently and the resulting protein was active. Although the sporulation efficiency of the recombinant strain was found to be reduced and its mobility impaired, overexpression of the lon gene triggered the production of endotoxin. Together with increased biofilm formation, recombinant strain exhibited significantly better adaptation to osmotic and heat shock stresses and UV exposure compared to wild type and the control strain with empty plasmid. This study suggested a possible link between Lon protease and the production of insecticide and stress response in B. thuringiensis and provides a platform for future studies focusing on enhancing bio-insecticidal production using this bacterium.

Indexed as

Bacillus thuringiensisProtease LaBacterial ProteinsEndotoxinsHemolysin ProteinsPlasmidsBacterial ProteinsEndotoxinsHemolysin ProteinsProtease La

Identifiers

PMID34272975
OpenAlexW3177961702

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.