Evidence map›Paper›PMID 26235787›Full record

ArticleScientific reports2015

Potential Role of Acetyl-CoA Synthetase (acs) and Malate Dehydrogenase (mae) in the Evolution of the Acetate Switch in Bacteria and Archaea.

Elliott P Barnhart, Marcella A McClure, Kiki Johnson, Sean Cleveland, Kristopher A Hunt, Matthew W Fields

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.3field-weighted citation impact, top 47% 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

10 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Microorganisms · 2024
    Article
  8. Article
  9. Methanogens: pushing the boundaries of biology.Emerging topics in life sciences · 2018
    Article
  10. Review
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 1 institution in 1 country.

Elliott P Barnhart1] Department of Microbiology and Immunology, Montana State University, Bozeman, MT, USA [2] Center for Biofilm Engineering, Montana State University, Bozeman, MT, USA [3] US Geological Survey, Helena, MT, USA.
Marcella A McClureDepartment of Microbiology and Immunology, Montana State University, Bozeman, MT, USA.
Kiki JohnsonDepartment of Microbiology and Immunology, Montana State University, Bozeman, MT, USA.
Sean ClevelandDepartment of Microbiology and Immunology, Montana State University, Bozeman, MT, USA.
Kristopher A Hunt1] Center for Biofilm Engineering, Montana State University, Bozeman, MT, USA [2] Department of Chemical and Biological Engineering, Montana State University, Bozeman, MT, USA.
Matthew W Fields1] Department of Microbiology and Immunology, Montana State University, Bozeman, MT, USA [2] Center for Biofilm Engineering, Montana State University, Bozeman, MT, USA [3] Energy Research Institute, Montana State University, Bozeman, MT, USA [4] ENIGMA, Lawrence Berkeley National Laboratory, Berkeley, CA, USA [5] National Center for Genome Resources, Santa Fe, NM, USA.
Montana State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although many Archaea have AMP-Acs (acetyl-coenzyme A synthetase) and ADP-Acs, the extant methanogenic genus Methanosarcina is the only identified Archaeal genus that can utilize acetate via acetate kinase (Ack) and phosphotransacetylase (Pta). Despite the importance of ack as the potential urkinase in the ASKHA phosphotransferase superfamily, an origin hypothesis does not exist for the acetate kinase in Bacteria, Archaea, or Eukarya. Here we demonstrate that Archaeal AMP-Acs and ADP-Acs contain paralogous ATPase motifs previously identified in Ack, which demonstrate a novel relation between these proteins in Archaea. The identification of ATPase motif conservation and resulting structural features in AMP- and ADP-acetyl-CoA synthetase proteins in this study expand the ASKHA superfamily to include acetyl-CoA synthetase. Additional phylogenetic analysis showed that Pta and MaeB sequences had a common ancestor, and that the Pta lineage within the halophilc archaea was an ancestral lineage. These results suggested that divergence of a duplicated maeB within an ancient halophilic, archaeal lineage formed a putative pta ancestor. These results provide a potential scenario for the establishment of the Ack/Pta pathway and provide novel insight into the evolution of acetate metabolism for all three domains of life.

Indexed as

Biological EvolutionAcetate-CoA LigaseAcetate KinaseAcetatesAmino Acid MotifsAmino Acid SequenceArchaeal ProteinsBacterial ProteinsConserved SequenceEvolution, MolecularHalobacterialesMalate DehydrogenaseMethanosarcinaPhosphate AcetyltransferasePhylogenySubstrate SpecificityAcetate-CoA LigaseAcetate KinaseAcetatesArchaeal ProteinsBacterial ProteinsMalate DehydrogenasePhosphate Acetyltransferase

Identifiers

PMID26235787
PMCPMC4522649
OpenAlexW1115611471

What OpenQuestion holds

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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.