Journal article
Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis
- Abstract:
- The canonical function of small heat-shock proteins (sHSPs) is to interact with proteins destabilized under conditions of cellular stress. While the breadth of interactions made by many sHSPs is well-known, there is currently little knowledge about what structural features of the interactors form the basis for their recognition. Here, we have identified 83 in vivo interactors of the sole sHSP in the cyanobacterium Synechocystis sp. PCC 6803, HSP16.6, reflective of stable associations with soluble proteins made under heat-shock conditions. By performing bioinformatic analyses on these interactors, we identify primary and secondary structural elements that are enriched relative to expectations from the cyanobacterial genome. In addition, by examining the Synechocystis interactors and comparing them with those identified to bind sHSPs in other prokaryotes, we show that sHSPs associate with specific proteins and biological processes. Our data are therefore consistent with a picture of sHSPs being broadly specific molecular chaperones that act to protect multiple cellular pathways.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 2.3MB, Terms of use)
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- Publisher copy:
- 10.1007/s12192-018-0884-3
Authors
- Publisher:
- Springer Netherlands
- Journal:
- Cell Stress and Chaperones More from this journal
- Volume:
- 23
- Issue:
- 4
- Pages:
- 723–732
- Publication date:
- 2018-02-23
- Acceptance date:
- 2018-02-01
- DOI:
- EISSN:
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1466-1268
- ISSN:
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1355-8145
- Pmid:
-
29476342
- Language:
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English
- Keywords:
- Pubs id:
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pubs:827705
- UUID:
-
uuid:3c937550-674b-4356-a032-57622a53c373
- Local pid:
-
pubs:827705
- Source identifiers:
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827705
- Deposit date:
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2018-03-03
Terms of use
- Copyright holder:
- Marklund et al
- Copyright date:
- 2018
- Notes:
-
Copyright © 2018 The Authors.
This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. A correction to this article is available online from Springer at: https://doi.org/10.1007/s12192-018-0901-6
- Licence:
- CC Attribution (CC BY)
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