Evidence map›Paper›PMID 23275245›Full record

ArticleJournal of bacteriology2013

Nutrient dependence of RNase E essentiality in Escherichia coli.

Masaru Tamura, Christopher J Moore, Stanley N Cohen

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.6field-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

15 citing papers in PubMed, 21 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

3 authors at 1 institution in 1 country.

Masaru TamuraDepartment of Genetics, School of Medicine, Stanford University, Stanford, California, USA.
Christopher J Moore
Stanley N Cohen
Stanford University · US

Funding

GENETICS TRAINING PROGRAM FOR PHD CANDIDATEST32GM007790 · NIGMS · STANFORD UNIVERSITY · PI BRUNET, ANNE, KINGSLEY, DAVID M · 1985 to 2020
$12.8M
Mechanisms of Antibiotic Resistance in BacteriaR01AI008619 · NIAID · STANFORD UNIVERSITY · PI COHEN, STANLEY N · 1985 to 2011
$5.3M
POLYADENYLATION OF RNA IN BACTERIAR01GM054158 · NIGMS · STANFORD UNIVERSITY · PI COHEN, STANLEY N · 1996 to 2006
$1.5M
GENETIC MECHANISMS IN BACTERIAL ANTIBIOTIC RESISTANCER37AI008619 · NIAID · STANFORD UNIVERSITY · PI COHEN, STANLEY N · 1986 to 1995
–
NIAID NIH HHS AI08619NIAID NIH HHS R01 AI008619NIGMS NIH HHS GM 54158NIGMS NIH HHS R01 GM054158NIGMS NIH HHS T32 GM007790
6 · The paper itself

Abstract

Escherichia coli cells normally require RNase E activity to form colonies (colony-forming ability [CFA]). The CFA-defective phenotype of cells lacking RNase E is partly reversed by overexpression of the related endoribonuclease RNase G or by mutation of the gene encoding the RNA helicase DeaD. We found that the carbon source utilization by rne deaD doubly mutant bacteria differs from that of rne(+) cells and from that of cells mutated in deaD alone and that the loss of rne function in these bacteria limits conversion of the glycolytic pathway product phosphoenolpyruvate to the tricarboxylic acid (TCA) cycle intermediate oxaloacetic acid. We show that the mechanism underlying this effect is reduced production of the enzyme phosphoenolpyruvate carboxylase (PPC) and that adventitious overexpression of PPC, which facilitates phosphoenolpyruvate utilization and connects the glycolytic pathway with the TCA cycle, restored CFA to rne deaD mutant bacteria cultured on carbon sources that otherwise were unable to sustain growth. We further show that bacteria producing full-length RNase E, which allows formation of degradosomes, have nutritional requirements different from those of cells supplied with only the N-terminal catalytic region of RNase E and that mitigation of RNase E deficiency by overexpression of a related RNase, RNase G, is also affected by carbon source. Our results reveal previously unsuspected effects of RNase E deficiency and degradosome formation on nutrient utilization by E. coli cells.

Indexed as

CarbonCitric Acid CycleEndoribonucleasesEscherichia coliEscherichia coli ProteinsGlycolysisHumansOxaloacetic AcidPhosphoenolpyruvatePhosphoenolpyruvate CarboxylaseRNA HelicasesCarbonEndoribonucleasesEscherichia coli ProteinsOxaloacetic AcidPhosphoenolpyruvatePhosphoenolpyruvate Carboxylaseribonuclease ERNA Helicasesrng protein, E coli

Identifiers

PMID23275245
PMCPMC3591997
OpenAlexW2083047016

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.