Evidence map›Paper›PMID 25947294›Full record

ArticleBMC microbiology2015

Enhanced oxygen consumption in Herbaspirillum seropedicae fnr mutants leads to increased NifA mediated transcriptional activation.

Marcelo Bueno Batista, Roseli Wassem, Fábio de Oliveira Pedrosa, Emanuel Maltempi de Souza, Ray Dixon, Rose Adele Monteiro

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Article
  3. Effect of point mutations on Herbaspirillum seropedicae NifA activity.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2015
    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 2 countries.

Marcelo Bueno BatistaDepartment of Biochemistry and Molecular Biology, Universidade Federal do Paraná, P.O. Box 19046, Curitiba, PR, 81531-990, Brazil. marcelo.buenobatista@gmail.com.
Roseli WassemDepartment of Genetics, Universidade Federal do Paraná, P.O. Box 19071, Curitiba, PR, 81531-990, Brazil. wassem@ufpr.br.
Fábio de Oliveira PedrosaDepartment of Biochemistry and Molecular Biology, Universidade Federal do Paraná, P.O. Box 19046, Curitiba, PR, 81531-990, Brazil. fpedrosa@ufpr.br.
Emanuel Maltempi de SouzaDepartment of Biochemistry and Molecular Biology, Universidade Federal do Paraná, P.O. Box 19046, Curitiba, PR, 81531-990, Brazil. souzaem@ufpr.br.
Ray DixonDepartment of Molecular Microbiology, John Innes Centre, Colney Lane, Norwich, NR4 7UH, UK. ray.dixon@jic.ac.uk.
Rose Adele MonteiroDepartment of Biochemistry and Molecular Biology, Universidade Federal do Paraná, P.O. Box 19046, Curitiba, PR, 81531-990, Brazil. roseadele@ufpr.br.
Universidade Federal do Paraná · BRJohn Innes Centre · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/E/J/00000016
6 · The paper itself

Abstract

backgroundOrthologous proteins of the Crp/Fnr family have been previously implicated in controlling expression and/or activity of the NifA transcriptional activator in some diazotrophs. This study aimed to address the role of three Fnr-like proteins from H. seropedicae SmR1 in controlling NifA activity and consequent NifA-mediated transcription activation.

resultsThe activity of NifA-dependent transcriptional fusions (nifA::lacZ and nifB::lacZ) was analysed in a series of H. seropedicae fnr deletion mutant backgrounds. We found that combined deletions in both the fnr1 and fnr3 genes lead to higher expression of both the nifA and nifB genes and also an increased level of nifH transcripts. Expression profiles of nifB under different oxygen concentrations, together with oxygen consumption measurements suggest that the triple fnr mutant has higher respiratory activity when compared to the wild type, which we believe to be responsible for greater stability of the oxygen sensitive NifA protein. This conclusion was further substantiated by measuring the levels of NifA protein and its activity in fnr deletion strains in comparison with the wild-type.

conclusionsFnr proteins are indirectly involved in controlling the activity of NifA in H. seropedicae, probably as a consequence of their influence on respiratory activity in relation to oxygen availability. Additionally we can suggest that there is some redundancy in the physiological function of the three Fnr paralogs in this organism, since altered respiration and effects on NifA activity are only observed in deletion strains lacking both fnr1 and fnr3.

Indexed as

Gene Expression Regulation, BacterialTranscriptional ActivationBacterial ProteinsHerbaspirillumIron-Sulfur ProteinsOxygenTranscription FactorsBacterial ProteinsIron-Sulfur ProteinsNifA protein, BacteriaOxygenTranscription Factors

Identifiers

PMID25947294
PMCPMC4422417
OpenAlexW1535977000

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.