Phylogeny and biogeography of the algal DMS-releasing enzyme in the global ocean.


Journal

ISME communications
ISSN: 2730-6151
Titre abrégé: ISME Commun
Pays: England
ID NLM: 9918205372406676

Informations de publication

Date de publication:
14 Jul 2023
Historique:
received: 21 02 2023
accepted: 29 06 2023
revised: 27 05 2023
medline: 15 7 2023
pubmed: 15 7 2023
entrez: 14 7 2023
Statut: epublish

Résumé

Phytoplankton produce the volatile dimethyl sulfide (DMS), an important infochemical mediating microbial interactions, which is also emitted to the atmosphere and affecting the global climate. Albeit the enzymatic source for DMS in eukaryotes was elucidated, namely a DMSP lyase (DL) called Alma1, we still lack basic knowledge regarding its taxonomic distribution. We defined unique sequence motifs which enable the identification of DL homologs (DLHs) in model systems and environmental populations. We used these motifs to predict DLHs in diverse algae by analyzing hundreds of genomic and transcriptomic sequences from model systems under stress conditions and from environmental samples. Our findings show that the DL enzyme is more taxonomically widespread than previously thought, as it is encoded by known algal taxa as haptophytes and dinoflagellates, but also by chlorophytes, pelagophytes and diatoms, which were conventionally considered to lack the DL enzyme. By exploring the Tara Oceans database, we showed that DLHs are widespread across the oceans and are predominantly expressed by dinoflagellates. Certain dinoflagellate DLHs were differentially expressed between the euphotic and mesopelagic zones, suggesting a functional specialization and an involvement in the metabolic plasticity of mixotrophic dinoflagellates. In specific regions as the Southern Ocean, DLH expression by haptophytes and diatoms was correlated with environmental drivers such as nutrient availability. The expanded repertoire of putative DL enzymes from diverse microbial origins and geographic niches suggests new potential players in the marine sulfur cycle and provides a foundation to study the cellular function of the DL enzyme in marine microbes.

Identifiants

pubmed: 37452148
doi: 10.1038/s43705-023-00280-2
pii: 10.1038/s43705-023-00280-2
pmc: PMC10349084
doi:

Types de publication

Journal Article

Langues

eng

Pagination

72

Subventions

Organisme : Israel Science Foundation (ISF)
ID : 1972/20

Informations de copyright

© 2023. The Author(s).

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Auteurs

Adva Shemi (A)

Department of Plant and Environmental Sciences, Weizmann Institute of Science, Rehovot, 7610001, Israel.

Shifra Ben-Dor (S)

Department of Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot, 7610001, Israel.

Ron Rotkopf (R)

Department of Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot, 7610001, Israel.

Orly Dym (O)

Structural Proteomics Unit, Faculty of Biochemistry, Weizmann Institute of Science, Rehovot, 7610001, Israel.

Assaf Vardi (A)

Department of Plant and Environmental Sciences, Weizmann Institute of Science, Rehovot, 7610001, Israel. assaf.vardi@weizmann.ac.il.

Classifications MeSH