Advanced

Probing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry.

Lambert, Wietske LU ; Rutsdottir, Gudrun LU ; Hussein, Rasha LU ; Bernfur, Katja LU ; Kjellström, Sven LU and Emanuelsson, Cecilia LU (2012) In Cell Stress & Chaperones
Abstract
Small heat-shock protein chaperones are important players in the protein quality control system of the cell, because they can immediately respond to partially unfolded proteins, thereby protecting the cell from harmful aggregates. The small heat-shock proteins can form large polydisperse oligomers that are exceptionally dynamic, which is implicated in their function of protecting substrate proteins from aggregation. Yet the mechanism of substrate recognition remains poorly understood, and little is known about what parts of the small heat-shock proteins interact with substrates and what parts of a partially unfolded substrate protein interact with the small heat-shock proteins. The transient nature of the interactions that prevent... (More)
Small heat-shock protein chaperones are important players in the protein quality control system of the cell, because they can immediately respond to partially unfolded proteins, thereby protecting the cell from harmful aggregates. The small heat-shock proteins can form large polydisperse oligomers that are exceptionally dynamic, which is implicated in their function of protecting substrate proteins from aggregation. Yet the mechanism of substrate recognition remains poorly understood, and little is known about what parts of the small heat-shock proteins interact with substrates and what parts of a partially unfolded substrate protein interact with the small heat-shock proteins. The transient nature of the interactions that prevent substrate aggregation rationalize probing this interaction by crosslinking mass spectrometry. Here, we used a workflow with lysine-specific crosslinking and offline nano-liquid chromatography matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry to explore the interaction between the plant small heat-shock protein Hsp21 and a thermosensitive model substrate protein, malate dehydrogenase. The identified crosslinks point at an interaction between the disordered N-terminal region of Hsp21 and the C-terminal presumably unfolding part of the substrate protein. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Cell Stress & Chaperones
publisher
Churchill Livingstone
external identifiers
  • wos:000312124500008
  • pmid:22851138
  • scopus:84870450357
ISSN
1466-1268
DOI
10.1007/s12192-012-0360-4
language
English
LU publication?
yes
id
3141d0f5-3e1b-45ba-be23-acb273a43e9b (old id 3047874)
date added to LUP
2012-09-10 15:52:38
date last changed
2017-06-04 03:54:31
@article{3141d0f5-3e1b-45ba-be23-acb273a43e9b,
  abstract     = {Small heat-shock protein chaperones are important players in the protein quality control system of the cell, because they can immediately respond to partially unfolded proteins, thereby protecting the cell from harmful aggregates. The small heat-shock proteins can form large polydisperse oligomers that are exceptionally dynamic, which is implicated in their function of protecting substrate proteins from aggregation. Yet the mechanism of substrate recognition remains poorly understood, and little is known about what parts of the small heat-shock proteins interact with substrates and what parts of a partially unfolded substrate protein interact with the small heat-shock proteins. The transient nature of the interactions that prevent substrate aggregation rationalize probing this interaction by crosslinking mass spectrometry. Here, we used a workflow with lysine-specific crosslinking and offline nano-liquid chromatography matrix-assisted laser desorption/ionization tandem time-of-flight mass spectrometry to explore the interaction between the plant small heat-shock protein Hsp21 and a thermosensitive model substrate protein, malate dehydrogenase. The identified crosslinks point at an interaction between the disordered N-terminal region of Hsp21 and the C-terminal presumably unfolding part of the substrate protein.},
  author       = {Lambert, Wietske and Rutsdottir, Gudrun and Hussein, Rasha and Bernfur, Katja and Kjellström, Sven and Emanuelsson, Cecilia},
  issn         = {1466-1268},
  language     = {eng},
  publisher    = {Churchill Livingstone},
  series       = {Cell Stress & Chaperones},
  title        = {Probing the transient interaction between the small heat-shock protein Hsp21 and a model substrate protein using crosslinking mass spectrometry.},
  url          = {http://dx.doi.org/10.1007/s12192-012-0360-4},
  year         = {2012},
}