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Subunit arrangement in the dodecameric chloroplast small heat shock protein Hsp21.

Lambert, Wietske ; Koeck, Philip J B ; Åhrman, Emma LU ; Purhonen, Pasi ; Cheng, Kimberley ; Elmlund, Dominika ; Hebert, Hans and Emanuelsson, Cecilia (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)
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organization
publishing date
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}},
}