Evidence map›Paper›PMID 19181799›Full record

ArticleJournal of bacteriology2009

Pathway of gamma-aminobutyrate metabolism in Rhizobium leguminosarum 3841 and its role in symbiosis.

Jurgen Prell, Alexandre Bourdès, Ramakrishnan Karunakaran, Miguel Lopez-Gomez, Philip Poole

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

34 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Aspartate aminotransferase ofMicrobiology (Reading, England) · 2024
    Article
  5. Article
  6. The Proteogenome of SymbioticMicroorganisms · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. How Rhizobia Adapt to the Nodule Environment.Journal of bacteriology · 2021
    Article
  11. Article
  12. Frontiers in microbiology · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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

5 authors at 2 institutions in 1 country.

Jurgen PrellDepartment of Molecular Microbiology, John Innes Centre, Norwich Research Park, Colney, United Kingdom.
Alexandre Bourdès
Ramakrishnan Karunakaran
Miguel Lopez-Gomez
Philip Poole
John Innes Centre · GBNorwich Research Park · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F013159/1Biotechnology and Biological Sciences Research Council BBS/B/02916
6 · The paper itself

Abstract

Pea plants incubated in 15N2 rapidly accumulated labeled gamma-aminobutyrate (GABA) in the plant cytosol and in bacteroids of Rhizobium leguminosarum bv. viciae 3841. Two pathways of GABA metabolism were identified in R. leguminosarum 3841. In the first, glutamate is formed by GABA aminotransferase (GabT), transferring the amino group from GABA to 2-oxoglutarate. In the second, alanine is formed by two omega-aminotransferases (OpaA and OpaB), transferring the amino group from GABA to pyruvate. While the gabT mutant and the gabT opaA double mutant grew on GABA as a nitrogen source, the final triple mutant did not. The semialdehyde released from GABA by transamination is oxidized by succinate semialdehyde dehydrogenase (GabD). Five of six potential GabD proteins in R. leguminosarum bv. viciae 3841 (GabD1, -D2, -D3, -D4, and -D5) were shown by expression analysis to have this activity. However, only mutations of GabD1, GabD2, and GabD4 were required to prevent utilization of GABA as the sole nitrogen source in culture. The specific enzyme activities of GabT, Opa, and GabD were highly elevated in bacteroids relative to cultured bacteria. This was due to elevated expression of gabT, opaA, gabD1, and gabD2 in nodules. Strains mutated in aminotransferase and succinate semialdehyde dehydrogenases (gabT, opaA, or opaB and gabD1, gabD2, or gabD4, respectively) that cannot use GABA in culture still fixed nitrogen on plants. While GABA catabolism alone is not essential for N2 fixation in bacteroids, it may have a role in energy generation and in bypassing the decarboxylating arm of the tricarboxylic acid cycle.

Indexed as

Biosynthetic PathwaysSymbiosisBacterial Proteinsgamma-Aminobutyric AcidMutationNitrogen FixationRhizobium leguminosarumSuccinate-Semialdehyde DehydrogenaseTransaminasesBacterial Proteinsgamma-Aminobutyric AcidSuccinate-Semialdehyde DehydrogenaseTransaminases

Identifiers

PMID19181799
PMCPMC2655508
OpenAlexW2133065762

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.