Publicação
Exploring dynamic structures of bionanocages
| Resumo: | Mini-ferritins also known as Dps (DNA-binding protein from starved cells) belong to the ferritin family. They are composed of 12 identical subunits forming a hollow quasi spherical structure with 9 nm outer diameter and 5 nm inner diameter. They can store up to 500 iron atoms per shell, being a vital piece in iron homeostasis. These proteins are able to oxidize Fe2+ ions using either H2O2 or O2, store it as a ferric mineral and release it in the ferrous form to the medium, when needed for various cellular processes. Dps proteins are also known to bind DNA thus protecting it from hazardous factors. In this Thesis the oligomeric states of Dps from Marinobacter (M.) hydrocarbonoclasticus were studied under different ionic strength conditions, in order to take advantage of the system for biotechnological uses. The present work has shown that the oligomerization is a dynamic process that can be controlled by the ionic strength and that the N- terminal tail is necessary for the dodecameric assembly. The DNA binding activity of Dps was also explored using DNA origami technology, which indicated that binding activity seems to occur in a wide range of pH values, being however not clear if there is a preferential binding to single or double stranded DNA. The biotechnological potential and versatility of this system to be employed as nanoreactor or a building block for the synthesis of novel enhanced supramolecular polymers were also demonstrated. The possibility to synthesise different metal nanoparticles/materials with constrained size inside the protein nanocage, using a simple procedure was proven. |
|---|---|
| Autores principais: | Jacinto, João Paulo Palma |
| Assunto: | Dps oligomerization DNA binding structural dynamics synchrotron radiation circular dichroism supramolecular protein polymer |
| Ano: | 2021 |
| País: | Portugal |
| Tipo de documento: | tese de doutoramento |
| Tipo de acesso: | acesso aberto |
| Instituição associada: | Universidade Nova de Lisboa |
| Idioma: | inglês |
| Origem: | Repositório Institucional da UNL |
| Resumo: | Mini-ferritins also known as Dps (DNA-binding protein from starved cells) belong to the ferritin family. They are composed of 12 identical subunits forming a hollow quasi spherical structure with 9 nm outer diameter and 5 nm inner diameter. They can store up to 500 iron atoms per shell, being a vital piece in iron homeostasis. These proteins are able to oxidize Fe2+ ions using either H2O2 or O2, store it as a ferric mineral and release it in the ferrous form to the medium, when needed for various cellular processes. Dps proteins are also known to bind DNA thus protecting it from hazardous factors. In this Thesis the oligomeric states of Dps from Marinobacter (M.) hydrocarbonoclasticus were studied under different ionic strength conditions, in order to take advantage of the system for biotechnological uses. The present work has shown that the oligomerization is a dynamic process that can be controlled by the ionic strength and that the N- terminal tail is necessary for the dodecameric assembly. The DNA binding activity of Dps was also explored using DNA origami technology, which indicated that binding activity seems to occur in a wide range of pH values, being however not clear if there is a preferential binding to single or double stranded DNA. The biotechnological potential and versatility of this system to be employed as nanoreactor or a building block for the synthesis of novel enhanced supramolecular polymers were also demonstrated. The possibility to synthesise different metal nanoparticles/materials with constrained size inside the protein nanocage, using a simple procedure was proven. |
|---|
Atividades financiadas
Não foram encontrados projetos financiados.