The unique self-assembly/disassembly property of Archaeoglobus fulgidus ferritin and its implications on molecular release from the protein cage
Copyright © 2015 Elsevier B.V. All rights reserved..
BACKGROUND: In conventional in vitro encapsulation of molecular cargo, the multi-subunit ferritin protein cages are disassembled in extremely acidic pH and re-assembled in the presence of highly concentrated cargo materials, which results in poor yields due to the low-pH treatment. In contrast, Archaeoglobus fulgidus open-pore ferritin (AfFtn) and its closed-pore mutant (AfFtn-AA) are present as dimeric species in neutral buffers that self-assemble into cage-like structure upon addition of metal ions.
METHODS: To understand the iron-mediated self-assembly and ascorbate-mediated disassembly properties, we studied the iron binding and release profile of the AfFtn and AfFtn-AA, and the corresponding oligomerization of their subunits.
RESULTS: Fe(2+) binding and conversion to Fe(3+) triggered the self-assembly of cage-like structures from dimeric species of AfFtn and AfFtn-AA subunits, while disassembly was induced by dissolving the iron core with reducing agents. The closed-pore AfFtn-AA has identical iron binding kinetics but lower iron release rates when compared to AfFtn. While the iron binding rate is proportional to Fe(2+) concentration, the iron release rate can be controlled by varying ascorbate concentrations.
CONCLUSION: The AfFtn and AfFtn-AA cages formed by iron mineralization could be disassembled by dissolving the iron core. The open-pores of AfFtn contribute to enhanced reductive iron release while the small channels located at the 3-fold symmetry axis (3-fold channels) are used for iron uptake.
GENERAL SIGNIFICANCE: The iron-mediated self-assembly/disassembly property of AfFtn offers a new set of molecular trigger for formation and dissociation of the protein cage, which can potentially regulate uptake and release of molecular cargo from protein cages.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2015 |
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| Erschienen: |
2015 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:1850 |
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| Enthalten in: |
Biochimica et biophysica acta - 1850(2015), 12 vom: 04. Dez., Seite 2544-51 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Sana, Barindra [VerfasserIn] |
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| Links: |
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| Themen: |
9007-73-2 |
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| Anmerkungen: |
Date Completed 11.01.2016 Date Revised 26.11.2016 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.bbagen.2015.08.019 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 100 | 1 | |a Sana, Barindra |e verfasserin |4 aut | |
| 245 | 1 | 4 | |a The unique self-assembly/disassembly property of Archaeoglobus fulgidus ferritin and its implications on molecular release from the protein cage |
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| 500 | |a Date Revised 26.11.2016 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2015 Elsevier B.V. All rights reserved. | ||
| 520 | |a BACKGROUND: In conventional in vitro encapsulation of molecular cargo, the multi-subunit ferritin protein cages are disassembled in extremely acidic pH and re-assembled in the presence of highly concentrated cargo materials, which results in poor yields due to the low-pH treatment. In contrast, Archaeoglobus fulgidus open-pore ferritin (AfFtn) and its closed-pore mutant (AfFtn-AA) are present as dimeric species in neutral buffers that self-assemble into cage-like structure upon addition of metal ions | ||
| 520 | |a METHODS: To understand the iron-mediated self-assembly and ascorbate-mediated disassembly properties, we studied the iron binding and release profile of the AfFtn and AfFtn-AA, and the corresponding oligomerization of their subunits | ||
| 520 | |a RESULTS: Fe(2+) binding and conversion to Fe(3+) triggered the self-assembly of cage-like structures from dimeric species of AfFtn and AfFtn-AA subunits, while disassembly was induced by dissolving the iron core with reducing agents. The closed-pore AfFtn-AA has identical iron binding kinetics but lower iron release rates when compared to AfFtn. While the iron binding rate is proportional to Fe(2+) concentration, the iron release rate can be controlled by varying ascorbate concentrations | ||
| 520 | |a CONCLUSION: The AfFtn and AfFtn-AA cages formed by iron mineralization could be disassembled by dissolving the iron core. The open-pores of AfFtn contribute to enhanced reductive iron release while the small channels located at the 3-fold symmetry axis (3-fold channels) are used for iron uptake | ||
| 520 | |a GENERAL SIGNIFICANCE: The iron-mediated self-assembly/disassembly property of AfFtn offers a new set of molecular trigger for formation and dissociation of the protein cage, which can potentially regulate uptake and release of molecular cargo from protein cages | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Binding kinetics | |
| 650 | 4 | |a Dissociation | |
| 650 | 4 | |a Molecular release | |
| 650 | 4 | |a Protein cage | |
| 650 | 4 | |a Release kinetics | |
| 650 | 4 | |a Self-assembly | |
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| 700 | 1 | |a Johnson, Eric |e verfasserin |4 aut | |
| 700 | 1 | |a Lim, Sierin |e verfasserin |4 aut | |
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