Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks.
Identifieur interne : 000813 ( Main/Merge ); précédent : 000812; suivant : 000814Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks.
Auteurs : Naoya Kobayashi [Japon] ; Kouichi Inano ; Kenji Sasahara ; Takaaki Sato [Japon] ; Keisuke Miyazawa [Japon] ; Takeshi Fukuma [Japon] ; Michael H. Hecht [États-Unis] ; Chihong Song [Japon] ; Kazuyoshi Murata [Japon] ; Ryoichi Arai [Japon]Source :
- ACS synthetic biology [ 2161-5063 ] ; 2018.
Descripteurs français
- KwdFr :
- Chromatographie sur gel, Diffraction des rayons X, Diffusion aux petits angles, Dénaturation des protéines, Escherichia coli (génétique), Ingénierie des protéines (), Microscopie à force atomique, Microscopie électronique à transmission, Nanostructures (), Protéines recombinantes (), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Repliement des protéines.
- MESH :
- génétique : Escherichia coli, Protéines recombinantes.
- métabolisme : Protéines recombinantes.
- Chromatographie sur gel, Diffraction des rayons X, Diffusion aux petits angles, Dénaturation des protéines, Ingénierie des protéines, Microscopie à force atomique, Microscopie électronique à transmission, Nanostructures, Protéines recombinantes, Repliement des protéines.
English descriptors
- KwdEn :
- Chromatography, Gel, Escherichia coli (genetics), Microscopy, Atomic Force, Microscopy, Electron, Transmission, Nanostructures (chemistry), Protein Denaturation, Protein Engineering (methods), Protein Refolding, Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Scattering, Small Angle, X-Ray Diffraction.
- MESH :
- chemical , chemistry : Recombinant Proteins.
- chemistry : Nanostructures.
- genetics : Escherichia coli, Recombinant Proteins.
- chemical , metabolism : Recombinant Proteins.
- methods : Protein Engineering.
- Chromatography, Gel, Microscopy, Atomic Force, Microscopy, Electron, Transmission, Protein Denaturation, Protein Refolding, Scattering, Small Angle, X-Ray Diffraction.
Abstract
The design of novel proteins that self-assemble into supramolecular complexes is important for development in nanobiotechnology and synthetic biology. Recently, we designed and created a protein nanobuilding block (PN-Block), WA20-foldon, by fusing an intermolecularly folded dimeric de novo WA20 protein and a trimeric foldon domain of T4 phage fibritin (Kobayashi et al., J. Am. Chem. Soc. 2015, 137, 11285). WA20-foldon formed several types of self-assembling nanoarchitectures in multiples of 6-mers, including a barrel-like hexamer and a tetrahedron-like dodecamer. In this study, to construct chain-like polymeric nanostructures, we designed de novo extender protein nanobuilding blocks (ePN-Blocks) by tandemly fusing two de novo binary-patterned WA20 proteins with various linkers. The ePN-Blocks with long helical linkers or flexible linkers were expressed in soluble fractions of Escherichia coli, and the purified ePN-Blocks were analyzed by native PAGE, size exclusion chromatography-multiangle light scattering (SEC-MALS), small-angle X-ray scattering (SAXS), and transmission electron microscopy. These results suggest formation of various structural homo-oligomers. Subsequently, we reconstructed hetero-oligomeric complexes from extender and stopper PN-Blocks by denaturation and refolding. The present SEC-MALS and SAXS analyses show that extender and stopper PN-Block (esPN-Block) heterocomplexes formed different types of extended chain-like conformations depending on their linker types. Moreover, atomic force microscopy imaging in liquid suggests that the esPN-Block heterocomplexes with metal ions further self-assembled into supramolecular nanostructures on mica surfaces. Taken together, the present data demonstrate that the design and construction of self-assembling PN-Blocks using de novo proteins is a useful strategy for building polymeric nanoarchitectures of supramolecular protein complexes.
DOI: 10.1021/acssynbio.8b00007
PubMed: 29690759
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Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks.</title><author><name sortKey="Kobayashi, Naoya" sort="Kobayashi, Naoya" uniqKey="Kobayashi N" first="Naoya" last="Kobayashi">Naoya Kobayashi</name><affiliation wicri:level="1"><nlm:affiliation>Exploratory Research Center on Life and Living Systems , National Institutes of Natural Sciences , Okazaki , Aichi 444-8787 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Exploratory Research Center on Life and Living Systems , National Institutes of Natural Sciences , Okazaki , Aichi 444-8787 </wicri:regionArea><wicri:noRegion>Aichi 444-8787 </wicri:noRegion></affiliation></author><author><name sortKey="Inano, Kouichi" sort="Inano, Kouichi" uniqKey="Inano K" first="Kouichi" last="Inano">Kouichi Inano</name></author><author><name sortKey="Sasahara, Kenji" sort="Sasahara, Kenji" uniqKey="Sasahara K" first="Kenji" last="Sasahara">Kenji Sasahara</name></author><author><name sortKey="Sato, Takaaki" sort="Sato, Takaaki" uniqKey="Sato T" first="Takaaki" last="Sato">Takaaki Sato</name><affiliation wicri:level="1"><nlm:affiliation>Center for Energy and Environmental Science , Interdisciplinary Cluster for Cutting Edge Research, Shinshu University , Nagano , Nagano 380-8553 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Center for Energy and Environmental Science , Interdisciplinary Cluster for Cutting Edge Research, Shinshu University , Nagano , Nagano 380-8553 </wicri:regionArea><wicri:noRegion>Nagano 380-8553 </wicri:noRegion></affiliation></author><author><name sortKey="Miyazawa, Keisuke" sort="Miyazawa, Keisuke" uniqKey="Miyazawa K" first="Keisuke" last="Miyazawa">Keisuke Miyazawa</name><affiliation wicri:level="1"><nlm:affiliation>Division of Electrical Engineering and Computer Science , Kanazawa University , Kanazawa , Ishikawa 920-1192 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Electrical Engineering and Computer Science , Kanazawa University , Kanazawa , Ishikawa 920-1192 </wicri:regionArea><wicri:noRegion>Ishikawa 920-1192 </wicri:noRegion></affiliation></author><author><name sortKey="Fukuma, Takeshi" sort="Fukuma, Takeshi" uniqKey="Fukuma T" first="Takeshi" last="Fukuma">Takeshi Fukuma</name><affiliation wicri:level="1"><nlm:affiliation>Division of Electrical Engineering and Computer Science , Kanazawa University , Kanazawa , Ishikawa 920-1192 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Electrical Engineering and Computer Science , Kanazawa University , Kanazawa , Ishikawa 920-1192 </wicri:regionArea><wicri:noRegion>Ishikawa 920-1192 </wicri:noRegion></affiliation></author><author><name sortKey="Hecht, Michael H" sort="Hecht, Michael H" uniqKey="Hecht M" first="Michael H" last="Hecht">Michael H. Hecht</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry , Princeton University , Princeton , New Jersey 08544 , United States.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry , Princeton University , Princeton , New Jersey 08544 </wicri:regionArea><wicri:noRegion>New Jersey 08544 </wicri:noRegion></affiliation></author><author><name sortKey="Song, Chihong" sort="Song, Chihong" uniqKey="Song C" first="Chihong" last="Song">Chihong Song</name><affiliation wicri:level="1"><nlm:affiliation>National Institute for Physiological Sciences , Okazaki , Aichi 444-8585 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>National Institute for Physiological Sciences , Okazaki , Aichi 444-8585 </wicri:regionArea><wicri:noRegion>Aichi 444-8585 </wicri:noRegion></affiliation></author><author><name sortKey="Murata, Kazuyoshi" sort="Murata, Kazuyoshi" uniqKey="Murata K" first="Kazuyoshi" last="Murata">Kazuyoshi Murata</name><affiliation wicri:level="1"><nlm:affiliation>National Institute for Physiological Sciences , Okazaki , Aichi 444-8585 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>National Institute for Physiological Sciences , Okazaki , Aichi 444-8585 </wicri:regionArea><wicri:noRegion>Aichi 444-8585 </wicri:noRegion></affiliation></author><author><name sortKey="Arai, Ryoichi" sort="Arai, Ryoichi" uniqKey="Arai R" first="Ryoichi" last="Arai">Ryoichi Arai</name><affiliation wicri:level="1"><nlm:affiliation>Division of Structural and Synthetic Biology , RIKEN Center for Life Science Technologies , Tsurumi , Yokohama 230-0045 , Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Division of Structural and Synthetic Biology , RIKEN Center for Life Science Technologies , Tsurumi , Yokohama 230-0045 </wicri:regionArea><wicri:noRegion>Yokohama 230-0045 </wicri:noRegion></affiliation></author></analytic><series><title level="j">ACS synthetic biology</title><idno type="eISSN">2161-5063</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatography, Gel</term><term>Escherichia coli (genetics)</term><term>Microscopy, Atomic Force</term><term>Microscopy, Electron, Transmission</term><term>Nanostructures (chemistry)</term><term>Protein Denaturation</term><term>Protein Engineering (methods)</term><term>Protein Refolding</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Scattering, Small Angle</term><term>X-Ray Diffraction</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chromatographie sur gel</term><term>Diffraction des rayons X</term><term>Diffusion aux petits angles</term><term>Dénaturation des protéines</term><term>Escherichia coli (génétique)</term><term>Ingénierie des protéines ()</term><term>Microscopie à force atomique</term><term>Microscopie électronique à transmission</term><term>Nanostructures ()</term><term>Protéines recombinantes ()</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Repliement des protéines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nanostructures</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Protein Engineering</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Gel</term><term>Microscopy, Atomic Force</term><term>Microscopy, Electron, Transmission</term><term>Protein Denaturation</term><term>Protein Refolding</term><term>Scattering, Small Angle</term><term>X-Ray Diffraction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie sur gel</term><term>Diffraction des rayons X</term><term>Diffusion aux petits angles</term><term>Dénaturation des protéines</term><term>Ingénierie des protéines</term><term>Microscopie à force atomique</term><term>Microscopie électronique à transmission</term><term>Nanostructures</term><term>Protéines recombinantes</term><term>Repliement des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The design of novel proteins that self-assemble into supramolecular complexes is important for development in nanobiotechnology and synthetic biology. Recently, we designed and created a protein nanobuilding block (PN-Block), WA20-foldon, by fusing an intermolecularly folded dimeric de novo WA20 protein and a trimeric foldon domain of T4 phage fibritin (Kobayashi et al., J. Am. Chem. Soc. 2015, 137, 11285). WA20-foldon formed several types of self-assembling nanoarchitectures in multiples of 6-mers, including a barrel-like hexamer and a tetrahedron-like dodecamer. In this study, to construct chain-like polymeric nanostructures, we designed de novo extender protein nanobuilding blocks (ePN-Blocks) by tandemly fusing two de novo binary-patterned WA20 proteins with various linkers. The ePN-Blocks with long helical linkers or flexible linkers were expressed in soluble fractions of Escherichia coli, and the purified ePN-Blocks were analyzed by native PAGE, size exclusion chromatography-multiangle light scattering (SEC-MALS), small-angle X-ray scattering (SAXS), and transmission electron microscopy. These results suggest formation of various structural homo-oligomers. Subsequently, we reconstructed hetero-oligomeric complexes from extender and stopper PN-Blocks by denaturation and refolding. The present SEC-MALS and SAXS analyses show that extender and stopper PN-Block (esPN-Block) heterocomplexes formed different types of extended chain-like conformations depending on their linker types. Moreover, atomic force microscopy imaging in liquid suggests that the esPN-Block heterocomplexes with metal ions further self-assembled into supramolecular nanostructures on mica surfaces. Taken together, the present data demonstrate that the design and construction of self-assembling PN-Blocks using de novo proteins is a useful strategy for building polymeric nanoarchitectures of supramolecular protein complexes.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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