Evidence map›Paper›PMID 24562786›Full record

ArticleExtremophiles : life under extreme conditions2014

Evidence for vital role of endo-β-N-acetylglucosaminidase in the resistance of Arthrobacter protophormiae RKJ100 towards elevated concentrations of o-nitrobenzoate.

Janmejay Pandey, Fazlurrahman Khan, Vivek Mahajan, Mahima Pant, Rakesh K Jain, Gunjan Pandey

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Article in Extremophiles : life under extreme conditions, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 47% of its field
1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Janmejay PandeyInstitute of Microbial Technology, Sector 39-A, Chandigarh, 160036, India, janmejay@curaj.ac.in.
Fazlurrahman Khan
Vivek Mahajan
Mahima Pant
Rakesh K Jain
Gunjan Pandey
Institute of Microbial Technology · INCommonwealth Scientific and Industrial Research Organisation · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arthrobacter protophormiae RKJ100 was previously characterized for its ability to tolerate extremely high concentrations of o-nitrobenzoate (ONB), a toxic xenobiotic environmental pollutant. The physiological responses of strain RKJ100 to ≥30 mM ONB indicated towards a resistance mechanism manifested via alteration of cell morphology and cell wall structure. In this study, we aim to characterize gene(s) involved in the resistance of strain RKJ100 towards extreme concentrations (i.e. 150 mM) of ONB. Transposon mutagenesis was carried out to generate a mutant library of strain RKJ100, which was then screened for ONB-sensitive mutants. A sensitive mutant was defined and selected as one that could not tolerate ≥30 mM ONB. Molecular and biochemical characterization of this mutant showed that the disruption of endo-β-N-acetylglucosaminidase (ENGase) gene caused the sensitivity. ENGase is an important enzyme for oligosaccharide processing and cell wall recycling in bacteria, fungi, plants and animals. Previous reports have already indicated several possible roles of this enzyme in cellular homeostasis. Results presented here provide the first evidence for its involvement in bacterial resistance towards extreme concentrations of a toxic xenobiotic compound and also suggest that strain RKJ100 employs ENGase as an important component in osmotic shock response for resisting extreme concentrations of ONB.

Indexed as

ArthrobacterBacterial ProteinsDrug Resistance, BacterialMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMutationNitrobenzoatesBacterial ProteinsMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseNitrobenzoates

Identifiers

PMID24562786
OpenAlexW1972999914

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.