Evidence map›Paper›PMID 18390659›Full record

ArticleJournal of bacteriology2008

Characterization of a novel methanol dehydrogenase in representatives of Burkholderiales: implications for environmental detection of methylotrophy and evidence for convergent evolution.

Marina G Kalyuzhnaya, Krassimira R Hristova, Mary E Lidstrom, Ludmila Chistoserdova

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

45 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Aerobic Utilization of Methanol for Microbial Growth and Production.Advances in biochemical engineering/biotechnology · 2022
    Article
  5. Article
  6. Article
  7. Genomic Analysis of Family UBA6911 (Group 18Applied and environmental microbiology · 2021
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Methanol Dehydrogenases as a Key Biocatalysts for Synthetic Methylotrophy.Frontiers in bioengineering and biotechnology · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Primary ColonizingApplied and environmental microbiology · 2018
    Article
  18. Genomics and Biochemistry of Metabolic Pathways for the CIndian journal of microbiology · 2018
    Article
  19. Metals and Methanotrophy.Applied and environmental microbiology · 2018
    Review
  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

4 authors at 2 institutions in 1 country.

Marina G KalyuzhnayaDepartment of Microbiology, University of Washington, Box 355014, Seattle, WA 98195, USA.
Krassimira R Hristova
Mary E Lidstrom
Ludmila Chistoserdova
University of Washington · USUniversity of California, Davis · US

Funding

Workshop on Environmental Technology Transfer and EntrepreneurshipP42ES004699 · NIEHS · UNIVERSITY OF CALIFORNIA DAVIS · PI HAMMOCK, BRUCE D · 1987 to 2021
$50.1M
NIEHS NIH HHS 5 P42 ES004699NIEHS NIH HHS P42 ES004699
6 · The paper itself

Abstract

Some members of Burkholderiales are able to grow on methanol but lack the genes (mxaFI) responsible for the well-characterized two-subunit pyrroloquinoline quinone-dependent quinoprotein methanol dehydrogenase that is widespread in methylotrophic Proteobacteria. Here, we characterized novel, mono-subunit enzymes responsible for methanol oxidation in four strains, Methyloversatilis universalis FAM5, Methylibium petroleiphilum PM1, and unclassified Burkholderiales strains RZ18-153 and FAM1. The enzyme from M. universalis FAM5 was partially purified and subjected to matrix-assisted laser desorption ionization-time of fight peptide mass fingerprinting. The resulting peptide spectrum was used to identify a gene candidate in the genome of M. petroleiphilum PM1 (mdh2) predicted to encode a type I alcohol dehydrogenase related to the characterized methanol dehydrogenase large subunits but at less than 35% amino acid identity. Homologs of mdh2 were amplified from M. universalis FAM5 and strains RZ18-153 and FAM1, and mutants lacking mdh2 were generated in three of the organisms. These mutants lost their ability to grow on methanol and ethanol, demonstrating that mdh2 is responsible for oxidation of both substrates. Our findings have implications for environmental detection of methylotrophy and indicate that this ability is widespread beyond populations possessing mxaF, the gene traditionally used as a genetic marker for environmental detection of methanol-oxidizing capability. Our findings also have implications for understanding the evolution of methanol oxidation, suggesting a convergence toward the enzymatic function for methanol oxidation in MxaF and Mdh2-type proteins.

Indexed as

Biological EvolutionAlcohol OxidoreductasesAmino Acid SequenceBacterial ProteinsBetaproteobacteriaGene Expression Regulation, BacterialMethanolMolecular Sequence DataMutationSpecies Specificityalcohol dehydrogenase (acceptor)Alcohol OxidoreductasesBacterial ProteinsMethanol

Identifiers

PMID18390659
PMCPMC2395034
OpenAlexW2060788363

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.