Subunit arrangement in the dodecameric chloroplast small heat shock protein Hsp21.
(2011) In Protein Science 20(2). p.291-301- Abstract
- Unfolding proteins are prevented from irreversible aggregation by small heat shock proteins (sHsps) through interactions that depend on a dynamic equilibrium between sHsp subunits and sHsp oligomers. A chloroplast-localized sHsp, Hsp21, provides protection to client proteins to increase plant stress resistance. Structural information is lacking concerning the oligomeric conformation of this sHsp. We here present a structure model of Arabidopsis thaliana Hsp21, obtained by homology modeling, single-particle electron microscopy, and lysine-specific chemical crosslinking. The model shows that the Hsp21 subunits are arranged in two hexameric discs, similar to a cytosolic plant sHsp homolog that has been structurally determined after... (More)
- Unfolding proteins are prevented from irreversible aggregation by small heat shock proteins (sHsps) through interactions that depend on a dynamic equilibrium between sHsp subunits and sHsp oligomers. A chloroplast-localized sHsp, Hsp21, provides protection to client proteins to increase plant stress resistance. Structural information is lacking concerning the oligomeric conformation of this sHsp. We here present a structure model of Arabidopsis thaliana Hsp21, obtained by homology modeling, single-particle electron microscopy, and lysine-specific chemical crosslinking. The model shows that the Hsp21 subunits are arranged in two hexameric discs, similar to a cytosolic plant sHsp homolog that has been structurally determined after crystallization. However, the two hexameric discs of Hsp21 are rotated by 25° in relation to each other, suggesting a role for global dynamics in dodecamer function. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1832521
- author
- Lambert, Wietske ; Koeck, Philip J B ; Åhrman, Emma LU ; Purhonen, Pasi ; Cheng, Kimberley ; Elmlund, Dominika ; Hebert, Hans and Emanuelsson, Cecilia
- organization
- publishing date
- 2011
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Protein Science
- volume
- 20
- issue
- 2
- pages
- 291 - 301
- publisher
- The Protein Society
- external identifiers
-
- wos:000286963300006
- pmid:21280121
- scopus:79251546073
- pmid:21280121
- ISSN
- 1469-896X
- DOI
- 10.1002/pro.560
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Division III (013230700), Division of Infection Medicine (BMC) (013024020), Connective Tissue Biology (013230151), Division of Infection Medicine (SUS) (013008000)
- id
- 734c1b22-3270-41f4-b21b-1833e21aec6d (old id 1832521)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/21280121?dopt=Abstract
- date added to LUP
- 2016-04-04 08:38:24
- date last changed
- 2022-02-13 06:31:41
@article{734c1b22-3270-41f4-b21b-1833e21aec6d, abstract = {{Unfolding proteins are prevented from irreversible aggregation by small heat shock proteins (sHsps) through interactions that depend on a dynamic equilibrium between sHsp subunits and sHsp oligomers. A chloroplast-localized sHsp, Hsp21, provides protection to client proteins to increase plant stress resistance. Structural information is lacking concerning the oligomeric conformation of this sHsp. We here present a structure model of Arabidopsis thaliana Hsp21, obtained by homology modeling, single-particle electron microscopy, and lysine-specific chemical crosslinking. The model shows that the Hsp21 subunits are arranged in two hexameric discs, similar to a cytosolic plant sHsp homolog that has been structurally determined after crystallization. However, the two hexameric discs of Hsp21 are rotated by 25° in relation to each other, suggesting a role for global dynamics in dodecamer function.}}, author = {{Lambert, Wietske and Koeck, Philip J B and Åhrman, Emma and Purhonen, Pasi and Cheng, Kimberley and Elmlund, Dominika and Hebert, Hans and Emanuelsson, Cecilia}}, issn = {{1469-896X}}, language = {{eng}}, number = {{2}}, pages = {{291--301}}, publisher = {{The Protein Society}}, series = {{Protein Science}}, title = {{Subunit arrangement in the dodecameric chloroplast small heat shock protein Hsp21.}}, url = {{http://dx.doi.org/10.1002/pro.560}}, doi = {{10.1002/pro.560}}, volume = {{20}}, year = {{2011}}, }