Evidence map›Paper›PMID 35729563›Full record

ArticleMicrobial cell factories2022

The TetR-type regulator AtsR is involved in multidrug response in Corynebacterium glutamicum.

Tao Su, Chengchuan Che, Jiyu Han, Yuying Zhao, Zihan Zhang, Guangdi An, Meiru Si, Can Chen

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

8 citing papers in PubMed, 11 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Tao Su *College of Life Sciences, Qufu Normal University, Qufu, Shandong, 273165, China. vincenttao2@163.com.
Chengchuan Che *College of Life Sciences, Qufu Normal University, Qufu, Shandong, 273165, China.
Jiyu HanCollege of Life Sciences, Qufu Normal University, Qufu, Shandong, 273165, China.
Yuying ZhaoCollege of Life Sciences, Qufu Normal University, Qufu, Shandong, 273165, China.
Zihan ZhangCollege of Life Sciences, Qufu Normal University, Qufu, Shandong, 273165, China.
Guangdi AnCollege of Life Sciences, Qufu Normal University, Qufu, Shandong, 273165, China.
Meiru SiCollege of Life Sciences, Qufu Normal University, Qufu, Shandong, 273165, China.
Can ChenKey Laboratory of Plant Genetics and Molecular Breeding, College of Life Science and Agronomy, Zhoukou Normal University, Zhoukou, Henan, 466001, China. chenc02@126.com.
Qufu Normal University · CNZhoukou Normal University · CN

Funding

Key Scientific and Technological Project of Henan Province, China 202102110189National Natural Science Foundation of China 31970034Training Plan of Young Backbone Teachers in Colleges and Universities of Henan Province, China 2021GGJS139
6 · The paper itself

Abstract

backgroundThe TetR (tetracycline repressor) family is one of the major transcription factor families that regulate expression of genes involved in bacterial antimicrobial resistance systems. NCgl0886 protein, designated as AtsR, is a member of the TetR family identified in Corynebacterium glutamicum, which is conserved in several species of the genera Corynebacterium, also including the well-known pathogen C. diphtheriae. AtsR is located at no far upstream of the identically oriented ncgl0884 gene, encoding a putative multidrug efflux pump protein, and in the same operon with ncgl0887, encoding a resistance, nodulation and cell division (RND) superfamily drug exporter. However, the role of AtsR is not clearly understood.

resultsHere we showed that dimeric AtsR directly repressed the expression of the ncgl0887-atsR operon, as well as indirectly controlled the ncgl0884 transcription. Antibiotics and toxic compounds induced the expression of ncgl0887-atsR operon. A perfect palindromic motif (5΄-TGCAA-N

conclusionsOur study revealed that AtsR was a redox regulator that sensed oxidative stress via thiol modification. The results obtained here will contribute to our understanding of the drug response mechanism not only in C. glutamicum but also in the related bacteria C. diphtheriae.

Indexed as

Corynebacterium glutamicumBacterial ProteinsGene Expression Regulation, BacterialHydrogen PeroxideRepressor ProteinsTranscription FactorsBacterial ProteinsHydrogen PeroxideRepressor ProteinsTranscription FactorsAtsRCorynebacterium glutamicumMultidrug resistanceTetR-type regulator

Identifiers

PMID35729563
PMCPMC9210681
OpenAlexW4283215204

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Registered trials

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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.