Advanced

Regulated protein aggregation, a mechanism to control the activity of the ClpXP adaptor protein YjbH.

Engman, Jakob LU and von Wachenfeldt, Claes LU (2015) In Molecular Microbiology 95(1). p.51-63
Abstract
Bacteria use stress response pathways to activate diverse target genes to react to a variety of stresses. The Bacillus subtilis Spx protein is a global transcriptional regulator that controls expression of more than 140 genes and operons in response to thiol-specific oxidative stress. Under non-stress conditions the concentration of Spx is kept low by proteolysis catalyzed by the ClpXP complex. Spx protein levels increase in response to disulfide stress, and decrease when the cells cope with the stress. The cytosolic adaptor protein YjbH is required to target Spx for efficient proteolysis by ClpXP. We demonstrate that YjbH aggregates in response to disulfide stress, that is, the YjbH protein is soluble under non-stressed conditions and... (More)
Bacteria use stress response pathways to activate diverse target genes to react to a variety of stresses. The Bacillus subtilis Spx protein is a global transcriptional regulator that controls expression of more than 140 genes and operons in response to thiol-specific oxidative stress. Under non-stress conditions the concentration of Spx is kept low by proteolysis catalyzed by the ClpXP complex. Spx protein levels increase in response to disulfide stress, and decrease when the cells cope with the stress. The cytosolic adaptor protein YjbH is required to target Spx for efficient proteolysis by ClpXP. We demonstrate that YjbH aggregates in response to disulfide stress, that is, the YjbH protein is soluble under non-stressed conditions and destabilized during stress leading to aggregation. Stress conditions (heat and ethanol) that cause severe perturbations in protein stability/folding also induced aggregation of YjbH and led to induction of Spx. By heterologous expression of a less aggregation prone YjbH homolog Spx induction was abolished. Thus we show that moderation of YjbH solubility is an important mechanism of signal transduction and represents a new mechanism of controlling the activity of adaptor proteins. (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
Molecular Microbiology
volume
95
issue
1
pages
51 - 63
publisher
Wiley-Blackwell
external identifiers
  • pmid:25353645
  • wos:000346656200004
  • scopus:84919339867
ISSN
1365-2958
DOI
10.1111/mmi.12842
language
English
LU publication?
yes
id
650cbd20-86a6-4399-a899-3a6d490dc170 (old id 4732982)
date added to LUP
2014-12-10 15:06:20
date last changed
2017-01-01 03:33:33
@article{650cbd20-86a6-4399-a899-3a6d490dc170,
  abstract     = {Bacteria use stress response pathways to activate diverse target genes to react to a variety of stresses. The Bacillus subtilis Spx protein is a global transcriptional regulator that controls expression of more than 140 genes and operons in response to thiol-specific oxidative stress. Under non-stress conditions the concentration of Spx is kept low by proteolysis catalyzed by the ClpXP complex. Spx protein levels increase in response to disulfide stress, and decrease when the cells cope with the stress. The cytosolic adaptor protein YjbH is required to target Spx for efficient proteolysis by ClpXP. We demonstrate that YjbH aggregates in response to disulfide stress, that is, the YjbH protein is soluble under non-stressed conditions and destabilized during stress leading to aggregation. Stress conditions (heat and ethanol) that cause severe perturbations in protein stability/folding also induced aggregation of YjbH and led to induction of Spx. By heterologous expression of a less aggregation prone YjbH homolog Spx induction was abolished. Thus we show that moderation of YjbH solubility is an important mechanism of signal transduction and represents a new mechanism of controlling the activity of adaptor proteins.},
  author       = {Engman, Jakob and von Wachenfeldt, Claes},
  issn         = {1365-2958},
  language     = {eng},
  number       = {1},
  pages        = {51--63},
  publisher    = {Wiley-Blackwell},
  series       = {Molecular Microbiology},
  title        = {Regulated protein aggregation, a mechanism to control the activity of the ClpXP adaptor protein YjbH.},
  url          = {http://dx.doi.org/10.1111/mmi.12842},
  volume       = {95},
  year         = {2015},
}