Evidence map›Paper›PMID 27164074›Full record

ArticleMolecules (Basel, Switzerland)2016

The Role of fadD19 and echA19 in Sterol Side Chain Degradation by Mycobacterium smegmatis.

Natalia Wrońska, Anna Brzostek, Rafał Szewczyk, Adrian Soboń, Jarosław Dziadek, Katarzyna Lisowska

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 98% 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

2 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Cells · 2024
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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

6 authors at 2 institutions in 1 country.

Natalia WrońskaDepartment of Industrial Microbiology and Biotechnology, Faculty of Biology and Environmental Protection, University of Lodz, 12/16 Banacha Street, 90-237 Lodz, Poland. nwronska@biol.uni.lodz.pl.
Anna BrzostekInstitute of Medical Biology, Polish Academy of Sciences, 106 Lodowa Street, 93-232 Lodz, Poland. abrzostek@cbm.pan.pl.
Rafał SzewczykDepartment of Industrial Microbiology and Biotechnology, Faculty of Biology and Environmental Protection, University of Lodz, 12/16 Banacha Street, 90-237 Lodz, Poland. rszewcz@biol.uni.lodz.pl.
Adrian SobońDepartment of Industrial Microbiology and Biotechnology, Faculty of Biology and Environmental Protection, University of Lodz, 12/16 Banacha Street, 90-237 Lodz, Poland. asobon@biol.uni.lodz.pl.
Jarosław DziadekInstitute of Medical Biology, Polish Academy of Sciences, 106 Lodowa Street, 93-232 Lodz, Poland. jdziadek@cbm.pan.pl.
Katarzyna LisowskaDepartment of Industrial Microbiology and Biotechnology, Faculty of Biology and Environmental Protection, University of Lodz, 12/16 Banacha Street, 90-237 Lodz, Poland. katalis@biol.uni.lodz.pl.
University of Łódź · PLInstitute for Medical Biology · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mycobacteria are able to degrade natural sterols and use them as a source of carbon and energy. Several genes which play an important role in cholesterol ring degradation have been described in Mycobacterium smegmatis. However, there are limited data describing the molecular mechanism of the aliphatic side chain degradation by Mycobacterium spp. In this paper, we analyzed the role of the echA19 and fadD19 genes in the degradation process of the side chain of cholesterol and β-sitosterol. We demonstrated that the M. smegmatis fadD19 and echA19 genes are not essential for viability. FadD19 is required in the initial step of the biodegradation of C-24 branched sterol side chains in Mycobacterium smegmatis mc²155, but not those carrying a straight chain like cholesterol. Additionally, we have shown that echA19 is not essential in the degradation of either substrate. This is the first report, to our knowledge, on the molecular characterization of the genes playing an essential role in C-24 branched side chain sterol degradation in M. smegmatis mc²155.

Indexed as

Bacterial ProteinsCholesterolEnoyl-CoA HydrataseLigasesMutationMycobacterium smegmatisSitosterolsSterolsBacterial ProteinsCholesterolEnoyl-CoA Hydratasegamma-sitosterolLigasesSitosterolsSterolscholesterolmicrobial sterol degradationM. smegmatissterol side-chain degradationβ-sitosterol

Identifiers

PMID27164074
PMCPMC6273163
OpenAlexW2346700586

What OpenQuestion holds

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LicenceCC BY
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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.