Evidence map›Paper›PMID 36828822›Full record

ArticleNature communications2023

Enzyme adaptation to habitat thermal legacy shapes the thermal plasticity of marine microbiomes.

Ramona Marasco, Marco Fusi, Cristina Coscolín, Alan Barozzi, David Almendral, Rafael Bargiela, Christina Gohlke Neé Nutschel, Christopher Pfleger, Jonas Dittrich, Holger Gohlke and 7 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.9field-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

11 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Highly efficient chitinase production fromFrontiers in microbiology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Microbial adaptability in changing environments.Nature reviews. Microbiology · 2024
    Article
  9. Article
  10. Article
  11. 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

17 authors at 8 institutions in 5 countries.

Ramona Marasco *Biological and Environmental Sciences and Engineering Division (BESE), Red Sea Research Centre (RSRC), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID 0000-0003-4776-7519
Marco Fusi *Biological and Environmental Sciences and Engineering Division (BESE), Red Sea Research Centre (RSRC), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID 0000-0001-7433-2487
Cristina Coscolín *Instituto de Catalisis y Petroleoquimica (ICP), CSIC, Madrid, Spain.ORCID 0000-0002-2117-8911
Alan BarozziBiological and Environmental Sciences and Engineering Division (BESE), Red Sea Research Centre (RSRC), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.ORCID 0000-0002-1090-1131
David AlmendralInstituto de Catalisis y Petroleoquimica (ICP), CSIC, Madrid, Spain.
Rafael BargielaCentre for Environmental Biotechnology, School of Natural Sciences, Bangor University, Deiniol Rd, Bangor, UK.
Christina Gohlke Neé NutschelInstitute of Bio- and Geosciences (IBG-4: Bioinformatics), Forschungszentrum Jülich GmbH, Jülich, Germany.
Christopher PflegerMathematisch-Naturwissenschaftliche Fakultät, Institut für Pharmazeutische und Medizinische Chemie, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.
Jonas DittrichMathematisch-Naturwissenschaftliche Fakultät, Institut für Pharmazeutische und Medizinische Chemie, Heinrich-Heine-Universität Düsseldorf, Düsseldorf, Germany.ORCID 0000-0003-2377-2268
Holger GohlkeInstitute of Bio- and Geosciences (IBG-4: Bioinformatics), Forschungszentrum Jülich GmbH, Jülich, Germany.
Ruth MatesanzSpectroscopy Laboratory, Centro de Investigaciones Biologicas Margarita Salas (CIB), CSIC, Madrid, Spain.
Sergio Sanchez-CarrilloInstituto de Catalisis y Petroleoquimica (ICP), CSIC, Madrid, Spain.ORCID 0000-0002-9271-7484
Francesca MapelliDepartment of Food Environmental and Nutritional Sciences, University of Milan, Milan, Italy.ORCID 0000-0002-2928-6538
Tatyana N ChernikovaCentre for Environmental Biotechnology, School of Natural Sciences, Bangor University, Deiniol Rd, Bangor, UK.
Peter N GolyshinCentre for Environmental Biotechnology, School of Natural Sciences, Bangor University, Deiniol Rd, Bangor, UK.ORCID 0000-0002-5433-0350
Manuel FerrerInstituto de Catalisis y Petroleoquimica (ICP), CSIC, Madrid, Spain. mferrer@icp.csic.es.ORCID 0000-0003-4962-4714
Daniele DaffonchioBiological and Environmental Sciences and Engineering Division (BESE), Red Sea Research Centre (RSRC), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia. daniele.daffonchio@kaust.edu.sa.ORCID 0000-0003-0947-925X
Instituto de Catálisis y Petroleoquímica · ESBangor University · GBKing Abdullah University of Science and Technology · SAForschungszentrum Jülich · DEHeinrich Heine University Düsseldorf · DECentro de Investigaciones Biológicas Margarita Salas · ESEdinburgh Napier University · GBUniversity of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microbial communities respond to temperature with physiological adaptation and compositional turnover. Whether thermal selection of enzymes explains marine microbiome plasticity in response to temperature remains unresolved. By quantifying the thermal behaviour of seven functionally-independent enzyme classes (esterase, extradiol dioxygenase, phosphatase, beta-galactosidase, nuclease, transaminase, and aldo-keto reductase) in native proteomes of marine sediment microbiomes from the Irish Sea to the southern Red Sea, we record a significant effect of the mean annual temperature (MAT) on enzyme response in all cases. Activity and stability profiles of 228 esterases and 5 extradiol dioxygenases from sediment and seawater across 70 locations worldwide validate this thermal pattern. Modelling the esterase phase transition temperature as a measure of structural flexibility confirms the observed relationship with MAT. Furthermore, when considering temperature variability in sites with non-significantly different MATs, the broadest range of enzyme thermal behaviour and the highest growth plasticity of the enriched heterotrophic bacteria occur in samples with the widest annual thermal variability. These results indicate that temperature-driven enzyme selection shapes microbiome thermal plasticity and that thermal variability finely tunes such processes and should be considered alongside MAT in forecasting microbial community thermal response.

Indexed as

MicrobiotaAdaptation, PhysiologicalBacteriaEsterasesSeawaterTemperatureEsterases

Identifiers

PMID36828822
PMCPMC9958047
OpenAlexW4321787068

What OpenQuestion holds

Textmetadata
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.