Unveiling hidden functions: 3D Structure prediction of the enigmatic Dinoflagellate dark proteome

 Stage · Stage M2  · 6 mois    Bac+5 / Master   Institut de Systématique Évolution et Biodiversité (ISYEB), equipe Atelier de Bioinformatique (ABI) · Paris 05 (France)  665

 Date de prise de poste : 6 janvier 2025

Mots-Clés

comparative genomics microbial diversity protein 3D structure

Description

Dinoflagellates are a diverse and ecologically important group of unicellular eukaryotes that play key roles in marine ecosystems. They are primary producers in phytoplankton and coral reef symbionts, and some of them are drivers of harmful algal blooms [1,2]. Alongside their remarkable biological innovations and trophic diversity [3], Dinoflagellate genomes remain among the most enigmatic in the eukaryotic domain, characterized by unusual features such as permanently condensed chromosomes, extensive gene duplication and atypical transcriptional regulation [4–6]. A significant proportion of dinoflagellate coding potential remains uncharacterized because of their very low similitude at the sequence level to reference protein databases[7]. These enigmatic proteins, which constitute their dark proteome, are key to understanding the molecular basis of their biological innovations and ecological success. To reduce this gap, in the framework of the ANR project “Exploring the functional diversity and genomic novelty of Dinoflagellates through the lens of their evolution and ecology”[8] we have compiled a dataset of diverse dinoflagellate proteomes and reconstructed gene families. Using sequence to sequence comparisons we have observed a number of protein coding gene families conserved and duplicated throughout the evolutionary history of dinoflagellate species potentially representing lineage innovations that have no sequence similarity to comprehensive annotation databases. Because the three-dimensional (3D) structure of a protein is more conserved than its sequence, comparing 3D structures offers a more sensitive way of identifying distant homologous proteins[9,10]. Therefore, we aim to better understand the origin and function of these conserved but enigmatic dinoflagellate proteins combining recently developed 3D protein structure prediction and structural homology search methods[11,12].
The particular objectives are :(1) Exploring gene families without annotations and originated and/or duplicated throughout the evolutionary history of dinoflagellates and investigate their features (disorder, transmembrane segments, cellular localization, etc), (2) Using 3D structure prediction methods on these prioritized lineage-specific proteins and (3) Looking for structural homologs of these proteins into 3D structure databases to find remote homologues that give us insights into their origin and functions and reveal potential novel protein folds originated in this eukaryotic lineage.

Références (iauthored by the supervising team)
1.
Guidi L, Chaffron S, Bittner L, Eveillard D, Larhlimi A, Roux S, et al. Plankton networks driving carbon export in the oligotrophic ocean. Nature. 2016;532: 465–470.
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7.
Meng A, Corre E, Probert I, Gutierrez-Rodriguez A, Siano R, Annamale A,Alberti A, Da Silva C, Wincker P, Le Crom S, Not . and Bittner L. Analysis of the genomic basis of functional diversity in dinoflagellates using a transcriptome-based sequence similarity network. Mol Ecol. 2018;27: 2365–2380.
8. Explorer la DIVErsité fonctionnelle et la nouveauté génomique des DINOflagellés à travers le prisme de leur évolution et de leur écologie. In: Agence nationale de la recherche granted to Lucie Bittner. [cited 1 Oct 2025]. Available: https://anr.fr/Projet-ANR-24-CE02-0557
9. Illergård K, Ardell DH, Elofsson A. Structure is three to ten times more conserved than sequence-a study of structural response in protein cores. Proteins. 2009;77: 499–508.
10.
Romei M, Carpentier M, Chomilier J, Lecointre G. Origins and functional significance of eukaryotic protein folds. J Mol Evol. 2023;91: 854–864.
11. Durairaj J, Waterhouse AM, Mets T, Brodiazhenko T, Abdullah M, Studer G, et al. Uncovering new families and folds in the natural protein universe. Nature. 2023;622: 646–653.
12. Barrio-Hernandez I, Yeo J, Jänes J, Wein T, Varadi M, Velankar S, et al. Clustering predicted structures at the scale of the known protein universe. bioRxiv. 2023. doi:10.1101/2023.03.09.531927

Candidature

Procédure : Send an email with your CV and a motivation letter to : jazmin.blazsanchez@mnhn.fr and lucie.bittner@mnhn.fr

Date limite : 1 janvier 2026

Contacts

 Jazmin Blaz
 jaNOSPAMzmin.blazsanchez@mnhn.fr

 Lucie Bittner
 luNOSPAMcie.bittner@mnhn.fr

Offre publiée le 16 octobre 2025, affichage jusqu'au 1 janvier 2026