Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis
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 th...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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Springer Netherlands
2018
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| _version_ | 1797063879318044672 |
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| author | Marklund, E Zhang, Y Basha, E Benesch, J Vierling, E |
| author_facet | Marklund, E Zhang, Y Basha, E Benesch, J Vierling, E |
| author_sort | Marklund, E |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T21:06:16Z |
| format | Journal article |
| id | oxford-uuid:3c937550-674b-4356-a032-57622a53c373 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:06:16Z |
| publishDate | 2018 |
| publisher | Springer Netherlands |
| record_format | dspace |
| spelling | oxford-uuid:3c937550-674b-4356-a032-57622a53c3732022-03-26T14:14:23ZStructural and functional aspects of the interaction partners of the small heat-shock protein in SynechocystisJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3c937550-674b-4356-a032-57622a53c373EnglishSymplectic Elements at OxfordSpringer Netherlands2018Marklund, EZhang, YBasha, EBenesch, JVierling, EThe 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. |
| spellingShingle | Marklund, E Zhang, Y Basha, E Benesch, J Vierling, E Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis |
| title | Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis |
| title_full | Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis |
| title_fullStr | Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis |
| title_full_unstemmed | Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis |
| title_short | Structural and functional aspects of the interaction partners of the small heat-shock protein in Synechocystis |
| title_sort | structural and functional aspects of the interaction partners of the small heat shock protein in synechocystis |
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