Phylogeny and biogeography of the algal DMS-releasing enzyme
Abstract
Phytoplankton produce the volatile dimethyl sulfide (DMS), an important infochemical, which is 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 taxonomy and biogeographic 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 in marine microbes.
02 /Specification & Classification
Click any tag to browse matching papers- Assay
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- DddY is a bacterial dimethylsulfoniopropionate lyase representing a new cupin enzyme superfamily with unknown primary function
Lei Lei, Uria Alcolombri, Dan S Tawfik·bioRxiv·Jul 9, 2017
- Novel enzyme for dimethyl sulfide-releasing in bacteria reveals a missing route in the marine sulfur cycle
C.-Y. Li, X.-J. Wang, … Y.-Z. Zhang·bioRxiv·Oct 29, 2020
- Chemosynthetic Symbioses as Hidden Hubs of DMSP and Organosulfur Cycling in Marine Sediments
Eileen Kröber, Kristina Weinert, … Nicole Dubilier·bioRxiv·Dec 5, 2025
- Native or promiscuous? Analyzing putative dimethylsulfoniopropionate lyases using a substrate proofing approach
Lei Lei, Kesava Phaneendra Cherukuri, … Dan S. Tawfik·bioRxiv·Jul 27, 2017
- Evolutionary history of dimethylsulfoniopropionate (DMSP) demethylation enzyme DmdA in marine bacteria
L. Hernández Javier, A. Vicens, … J. M. González·bioRxiv·Oct 15, 2019
- Bacterial virulence against an oceanic bloom-forming phytoplankter is mediated by algal DMSP
N. Barak-Gavish, M. J. Frada, … A. Vardi·bioRxiv·May 15, 2018