Diversity and evolution of tyrosinase enzymes involved in the adhesive systems of mussels and tubeworms

Mussels and tubeworms have evolved similar adhesive systems to cope with the hydrodynamics of intertidal environments. Both secrete adhesive proteins rich in DOPA, a post-translationally modified amino acid playing essential roles in their permanent adhesion. DOPA is produced by the hydroxylation of tyrosine residues by tyrosinase enzymes, which can also oxidize it further into dopaquinone. We have compiled a catalog of the tyrosinases potentially involved in the adhesive systems of <i>Mytilus edulis</i> and <i>Sabellaria alveolata</i>. Some were shown to be expressed in the adhesive glands, with a high gland specificity in mussels but not in tubeworms. The diversity of tyrosinases identified in the two species suggests the coexistence of different enzymatic activities and substrate specificities. However, the exact role of the different enzymes needs to be further investigated. Phylogenetic analyses support the hypothesis of independent expansions and parallel evolution of tyrosinases involved in DOPA-based adhesion in both lineages.

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Publication Details

Journal
iScience
Published
2024-11-20
DOI
https://doi.org/10.1016/j.isci.2024.111443
Citations
8
Primary Topic
Marine Biology and Environmental Chemistry
Type
article
Field-Weighted Citation Impact
2.69

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article

Diversity and evolution of tyrosinase enzymes involved in the adhesive systems of mussels and tubeworms

Jérôme Delroisse, Bárbara Maldonado, Patrick Flammang, Ruddy Wattiez et al.
8 citations
iScience
Marine Biology and Environmental Chemistry
2.69
article

Diversity and evolution of tyrosinase enzymes involved in the adhesive systems of mussels and tubeworms

Jérôme Delroisse, Bárbara Maldonado, Patrick Flammang, Ruddy Wattiez, Cyril Mascolo, Pascal Jean Lopez, Emilie Duthoo, Cécile Van de Weerdt, Matthew J. Harrington, Fabien Sinot
article en
8 citations

Abstract

Mussels and tubeworms have evolved similar adhesive systems to cope with the hydrodynamics of intertidal environments. Both secrete adhesive proteins rich in DOPA, a post-translationally modified amino acid playing essential roles in their permanent adhesion. DOPA is produced by the hydroxylation of tyrosine residues by tyrosinase enzymes, which can also oxidize it further into dopaquinone. We have compiled a catalog of the tyrosinases potentially involved in the adhesive systems of <i>Mytilus edulis</i> and <i>Sabellaria alveolata</i>. Some were shown to be expressed in the adhesive glands, with a high gland specificity in mussels but not in tubeworms. The diversity of tyrosinases identified in the two species suggests the coexistence of different enzymatic activities and substrate specificities. However, the exact role of the different enzymes needs to be further investigated. Phylogenetic analyses support the hypothesis of independent expansions and parallel evolution of tyrosinases involved in DOPA-based adhesion in both lineages.

iScienceVol. 27(12)
Centre National de la Recherche Scientifique (FR), University of Mons (BE), University of Liège (BE), Sorbonne Université (FR), Biologie des Organismes et Écosystèmes Aquatiques (FR), Institut de Recherche pour le Développement (FR), McGill University (CA)
Labex DRIIHM, Agence Nationale de la Recherche, Fonds De La Recherche Scientifique - FNRS, Fonds pour la Formation à la Recherche dans l’Industrie et dans l’Agriculture
Life below water
Openalex Percentile: Top 10%
Marine Biology and Environmental Chemistry
2.69
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