Evidence map›Paper›PMID 37439834›Full record

ArticleApplied microbiology and biotechnology2023

Genetic analysis of acyl-CoA carboxylases involved in lipid accumulation in Rhodococcus jostii RHA1.

Andrea L Livieri, Facundo Colaccini, Martin A Hernández, Gabriela Gago, Héctor M Alvarez, Hugo Gramajo, Eduardo Rodriguez

Abstract read
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In one paragraph

Article in Applied microbiology and biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. (Pan)genomic analysis of twoMicrobiology spectrum · 2024
    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

7 authors at 3 institutions in 2 countries.

Andrea L LivieriInstituto de Biología Molecular y Celular de Rosario, Facultad de Ciencias Bioquímicas Y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina.
Facundo ColacciniInstituto de Biología Molecular y Celular de Rosario, Facultad de Ciencias Bioquímicas Y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina.
Martin A HernándezInstituto de Biociencias de La Patagonia, Facultad de Ciencias Naturales y Ciencias de La Salud, Universidad Nacional de La Patagonia San Juan Bosco y CONICET, Comodoro Rivadavia, Argentina.
Gabriela GagoInstituto de Biología Molecular y Celular de Rosario, Facultad de Ciencias Bioquímicas Y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina.
Héctor M AlvarezInstituto de Biociencias de La Patagonia, Facultad de Ciencias Naturales y Ciencias de La Salud, Universidad Nacional de La Patagonia San Juan Bosco y CONICET, Comodoro Rivadavia, Argentina.
Hugo GramajoInstituto de Biología Molecular y Celular de Rosario, Facultad de Ciencias Bioquímicas Y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina. gramajo@ibr-coniet.gov.ar.
Eduardo RodriguezInstituto de Biología Molecular y Celular de Rosario, Facultad de Ciencias Bioquímicas Y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Argentina. erodriguez@ibr-conicet.gov.ar.ORCID http://orcid.org/0009-0007-5444-4642
National University of Rosario · ARConsejo Nacional de Investigaciones Científicas y Técnicas · ARUniversitat Autònoma de Barcelona · ES

Funding

Agencia Nacional de Promoción Científica y Tecnológica PICT StartUp 2020-0038
6 · The paper itself

Abstract

In actinomycetes, the acyl-CoA carboxylases, including the so-called acetyl-CoA carboxylases (ACCs), are biotin-dependent enzymes that exhibit broad substrate specificity and diverse domain and subunit arrangements. Bioinformatic analyses of the Rhodococcus jostii RHA1 genome found that this microorganism contains a vast arrange of putative acyl-CoA carboxylases domains and subunits. From the thirteen putative carboxyltransferase domains, only the carboxyltransferase subunit RO01202 and the carboxyltransferase domain present in the multidomain protein RO04222 are highly similar to well-known essential ACC subunits from other actinobacteria. Mutant strains in each of these genes showed that none of these enzymes is essential for R. jostii growth in rich or in minimal media with high nitrogen concentration, presumably because of their partial overlapping activities. A mutant strain in the ro04222 gene showed a decrease in triacylglycerol and mycolic acids accumulation in rich and minimal medium, highlighting the relevance of this multidomain ACC in the biosynthesis of these lipids. On the other hand, RO01202, a carboxyltransferase domain of a putative ACC complex, whose biotin carboxylase and biotin carboxyl carrier protein domain were not yet identified, was found to be essential for R. jostii growth only in minimal medium with low nitrogen concentration. The results of this study have identified a new component of the TAG-accumulating machinery in the oleaginous R. jostii RHA1. While non-essential for growth and TAG biosynthesis in RHA1, the activity of RO04222 significantly contributes to lipogenesis during single-cell oil production. Furthermore, this study highlights the high functional diversity of ACCs in actinobacteria, particularly regarding their essentiality under different environmental conditions. KEY POINTS: • R. jostii possess a remarkable heterogeneity in their acyl-carboxylase complexes. • RO04222 is a multidomain acetyl-CoA carboxylase involved in lipid accumulation. • RO01202 is an essential carboxyltransferase only at low nitrogen conditions.

Indexed as

Carboxyl and Carbamoyl TransferasesRhodococcusCarbon-Carbon LigasesNitrogenTriglyceridesacyl-CoA carboxylaseCarbon-Carbon LigasesCarboxyl and Carbamoyl TransferasesNitrogenTriglyceridesAcetyl-CoA carboxylaseRhodococcusTriacylglycerol

Identifiers

PMID37439834
OpenAlexW4384120302

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.