The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein of Deinococcus radiodurans

Domenica Farci , Giulia Guadalupi , Katarzyna Bierla (1) , Ryszard Lobinski (1) , Dario Piano (2)

1 IPREM - Institut des sciences analytiques et de physico-chimie pour l'environnement et les materiaux
2 Int Inst Mol & Cell Biol, PL-02109 Warsaw, Poland

Surface (S)-layers are cryptic structures that coat the external surface of the bacterial cell in many species. The paracrystalline regularity of the S-layer is due to the self-assembling of one or more protein units. The property of self-assembling seems to be mediated by specific topologies of the S-layer proteins as well as the presence of specific ions that provide support in building and stabilizing the bi-dimensional S-layer organization. In the present study, we have investigated the self-assembling mechanism of the main S-layer protein of Deinococcus radiodurans (DR_2577) finding an unusual role played by Fe3+ and Cu2+ in the oligomerization of this protein. These findings may trace a structural and functional metallo-mediated convergence between the role of these metals in the assembling of the S-layer and their well-known roles in protecting against oxidative stress in D. radiodurans.

Mots clés: Deinococcus radiodurans; DR_2577; metal-binding domain; oligomerization; SlpA; S-layer deinoxanthin binding complex

Domaines: Chimie analytique; Chimie théorique et/ou physique; Polymères; Matériaux

Domenica Farci, Giulia Guadalupi, Katarzyna Bierla, Ryszard Lobinski, Dario Piano. The Role of Iron and Copper on the Oligomerization Dynamics of DR_2577, the Main S-Layer Protein of Deinococcus radiodurans. Frontiers in Microbiology, 2019, 10, pp.1450. ⟨10.3389/fmicb.2019.01450⟩. ⟨hal-02270978⟩