Cargando…
Characterizing the Dynamic Disassembly/Reassembly Mechanisms of Encapsulin Protein Nanocages
[Image: see text] Encapsulins, self-assembling icosahedral protein nanocages derived from prokaryotes, represent a versatile set of tools for nanobiotechnology. However, a comprehensive understanding of the mechanisms underlying encapsulin self-assembly, disassembly, and reassembly is lacking. Here,...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2021
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8757444/ https://www.ncbi.nlm.nih.gov/pubmed/35036749 http://dx.doi.org/10.1021/acsomega.1c05472 |
_version_ | 1784632681816915968 |
---|---|
author | Boyton, India Goodchild, Sophia C. Diaz, Dennis Elbourne, Aaron Collins-Praino, Lyndsey E. Care, Andrew |
author_facet | Boyton, India Goodchild, Sophia C. Diaz, Dennis Elbourne, Aaron Collins-Praino, Lyndsey E. Care, Andrew |
author_sort | Boyton, India |
collection | PubMed |
description | [Image: see text] Encapsulins, self-assembling icosahedral protein nanocages derived from prokaryotes, represent a versatile set of tools for nanobiotechnology. However, a comprehensive understanding of the mechanisms underlying encapsulin self-assembly, disassembly, and reassembly is lacking. Here, we characterize the disassembly/reassembly properties of three encapsulin nanocages that possess different structural architectures: T = 1 (24 nm), T = 3 (32 nm), and T = 4 (42 nm). Using spectroscopic techniques and electron microscopy, encapsulin architectures were found to exhibit varying sensitivities to the denaturant guanidine hydrochloride (GuHCl), extreme pH, and elevated temperature. While all three encapsulins showed the capacity to reassemble following GuHCl-induced disassembly (within 75 min), only the smallest T = 1 nanocage reassembled after disassembly in basic pH (within 15 min). Furthermore, atomic force microscopy revealed that all encapsulins showed a significant loss of structural integrity after undergoing sequential disassembly/reassembly steps. These findings provide insights into encapsulins’ disassembly/reassembly dynamics, thus informing their future design, modification, and application. |
format | Online Article Text |
id | pubmed-8757444 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-87574442022-01-14 Characterizing the Dynamic Disassembly/Reassembly Mechanisms of Encapsulin Protein Nanocages Boyton, India Goodchild, Sophia C. Diaz, Dennis Elbourne, Aaron Collins-Praino, Lyndsey E. Care, Andrew ACS Omega [Image: see text] Encapsulins, self-assembling icosahedral protein nanocages derived from prokaryotes, represent a versatile set of tools for nanobiotechnology. However, a comprehensive understanding of the mechanisms underlying encapsulin self-assembly, disassembly, and reassembly is lacking. Here, we characterize the disassembly/reassembly properties of three encapsulin nanocages that possess different structural architectures: T = 1 (24 nm), T = 3 (32 nm), and T = 4 (42 nm). Using spectroscopic techniques and electron microscopy, encapsulin architectures were found to exhibit varying sensitivities to the denaturant guanidine hydrochloride (GuHCl), extreme pH, and elevated temperature. While all three encapsulins showed the capacity to reassemble following GuHCl-induced disassembly (within 75 min), only the smallest T = 1 nanocage reassembled after disassembly in basic pH (within 15 min). Furthermore, atomic force microscopy revealed that all encapsulins showed a significant loss of structural integrity after undergoing sequential disassembly/reassembly steps. These findings provide insights into encapsulins’ disassembly/reassembly dynamics, thus informing their future design, modification, and application. American Chemical Society 2021-12-20 /pmc/articles/PMC8757444/ /pubmed/35036749 http://dx.doi.org/10.1021/acsomega.1c05472 Text en © 2021 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by-nc-nd/4.0/Permits non-commercial access and re-use, provided that author attribution and integrity are maintained; but does not permit creation of adaptations or other derivative works (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Boyton, India Goodchild, Sophia C. Diaz, Dennis Elbourne, Aaron Collins-Praino, Lyndsey E. Care, Andrew Characterizing the Dynamic Disassembly/Reassembly Mechanisms of Encapsulin Protein Nanocages |
title | Characterizing the Dynamic Disassembly/Reassembly
Mechanisms of Encapsulin Protein Nanocages |
title_full | Characterizing the Dynamic Disassembly/Reassembly
Mechanisms of Encapsulin Protein Nanocages |
title_fullStr | Characterizing the Dynamic Disassembly/Reassembly
Mechanisms of Encapsulin Protein Nanocages |
title_full_unstemmed | Characterizing the Dynamic Disassembly/Reassembly
Mechanisms of Encapsulin Protein Nanocages |
title_short | Characterizing the Dynamic Disassembly/Reassembly
Mechanisms of Encapsulin Protein Nanocages |
title_sort | characterizing the dynamic disassembly/reassembly
mechanisms of encapsulin protein nanocages |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8757444/ https://www.ncbi.nlm.nih.gov/pubmed/35036749 http://dx.doi.org/10.1021/acsomega.1c05472 |
work_keys_str_mv | AT boytonindia characterizingthedynamicdisassemblyreassemblymechanismsofencapsulinproteinnanocages AT goodchildsophiac characterizingthedynamicdisassemblyreassemblymechanismsofencapsulinproteinnanocages AT diazdennis characterizingthedynamicdisassemblyreassemblymechanismsofencapsulinproteinnanocages AT elbourneaaron characterizingthedynamicdisassemblyreassemblymechanismsofencapsulinproteinnanocages AT collinsprainolyndseye characterizingthedynamicdisassemblyreassemblymechanismsofencapsulinproteinnanocages AT careandrew characterizingthedynamicdisassemblyreassemblymechanismsofencapsulinproteinnanocages |