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贻贝和管虫附着系统中酪氨酸酶的多样性与进化。

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

作者信息

Duthoo Emilie, Delroisse Jérôme, Maldonado Barbara, Sinot Fabien, Mascolo Cyril, Wattiez Ruddy, Lopez Pascal Jean, Van de Weerdt Cécile, Harrington Matthew J, Flammang Patrick

机构信息

Biology of Marine Organisms and Biomimetics Unit, Research Institute for Biosciences, University of Mons, Place du Parc 23, 7000 Mons, Belgium.

Laboratory of Cellular and Molecular Immunology, GIGA Institute, University of Liège, 11 avenue de l'hôpital, 4000 Liège, Belgium.

出版信息

iScience. 2024 Nov 20;27(12):111443. doi: 10.1016/j.isci.2024.111443. eCollection 2024 Dec 20.

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 and . 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.

摘要

贻贝和管虫已经进化出相似的粘附系统来应对潮间带环境的流体动力学。它们都会分泌富含多巴(DOPA)的粘附蛋白,多巴是一种翻译后修饰的氨基酸,在它们的永久粘附中起着至关重要的作用。多巴由酪氨酸酶将酪氨酸残基羟基化产生,酪氨酸酶也能将其进一步氧化成多巴醌。我们编制了一份可能参与贻贝和管虫粘附系统的酪氨酸酶目录。其中一些被证明在粘附腺中表达,在贻贝中具有很高的腺体特异性,但在管虫中则不然。在这两个物种中鉴定出的酪氨酸酶的多样性表明不同的酶活性和底物特异性共存。然而,不同酶的确切作用还有待进一步研究。系统发育分析支持这两个谱系中参与基于多巴的粘附的酪氨酸酶独立扩张和平行进化的假说。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/05e0/11667028/283a40e72584/fx1.jpg

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