Journal article
Engineering of a polydisperse small heat-shock protein reveals conserved motifs of oligomer plasticity
- Abstract:
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Small heat-shock proteins (sHSPs) are molecular chaperones that bind partially and globally unfolded states of their client proteins. Previously, we discovered that the archaeal Hsp16.5, which forms ordered and symmetric 24-subunit oligomers, can be engineered to transition to an ordered and symmetric 48-subunit oligomer by insertion of a peptide from human HspB1 (Hsp27). Here, we uncovered the existence of an array of oligomeric states (30–38 subunits) that can be populated as a consequence ...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Files:
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(Accepted manuscript, pdf, 3.3MB)
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- Publisher copy:
- 10.1016/j.str.2018.05.015
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Authors
Funding
+ Biotechnology and Biological Sciences Research Council
More from this funder
Funding agency for:
Benesch, J
Grant:
BB/L017067/1
+ Biotechnology and Biological Sciences Research Council
More from this funder
Funding agency for:
Chandler, S
Grant:
BB/L017067/1
Bibliographic Details
- Publisher:
- Elsevier Publisher's website
- Journal:
- Structure Journal website
- Volume:
- 26
- Issue:
- 8
- Pages:
- 1-11
- Publication date:
- 2018-01-01
- Acceptance date:
- 2018-05-18
- DOI:
- EISSN:
-
1878-4186
- ISSN:
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0969-2126
- Source identifiers:
-
859120
Item Description
- Keywords:
- Pubs id:
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pubs:859120
- UUID:
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uuid:b9b9ac13-5fa2-47ca-be46-a364528539b3
- Local pid:
- pubs:859120
- Deposit date:
- 2018-06-28
Terms of use
- Copyright holder:
- Elsevier ltd
- Copyright date:
- 2018
- Notes:
- © 2018 Elsevier Ltd. This is the accepted manuscript version of the article. The final version is available online from Elsevier at: https://doi.org/10.1016/j.str.2018.05.015
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