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Inducing the oxidative stress response in Escherichia coli improves the quality of a recombinant protein: magnesium chelatase ChlH

Muller, A. H.; Sawicki, A.; Zhou, S.; Tabrizi, S. T.; Luo, M.; Hansson, Mats LU and Willows, R. D. (2014) In Protein Expression and Purification 101. p.61-67
Abstract
The approximately 150kDa ChlH subunit of magnesium chelatase from Oryza sativa, Hordeum vulgare and Chlamydomonas reinhardtii have been heterologously expressed in Escherichiacoli. The active soluble protein is found as both a multimeric and a monomeric form. The multimeric ChlH appears to be oxidatively damaged but monomer production is favoured in growth conditions that are known to cause an oxidative stress response in E.coli. Inducing an oxidative stress response may be of general utility to improve the quality of proteins expressed in E. coli. The similar responses of ChlH's from the three different species suggest that oligomerization of oxidatively damaged ChlH may have a functional role in the chloroplast, possibly as a signal of... (More)
The approximately 150kDa ChlH subunit of magnesium chelatase from Oryza sativa, Hordeum vulgare and Chlamydomonas reinhardtii have been heterologously expressed in Escherichiacoli. The active soluble protein is found as both a multimeric and a monomeric form. The multimeric ChlH appears to be oxidatively damaged but monomer production is favoured in growth conditions that are known to cause an oxidative stress response in E.coli. Inducing an oxidative stress response may be of general utility to improve the quality of proteins expressed in E. coli. The similar responses of ChlH's from the three different species suggest that oligomerization of oxidatively damaged ChlH may have a functional role in the chloroplast, possibly as a signal of oxidative stress or damage. (Less)
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author
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Contribution to journal
publication status
published
subject
keywords
Protein Multimerization/*physiology, Oxidative Stress/*physiology, Oxidation-Reduction, Oryza sativa/enzymology, Lyases/*biosynthesis/genetics/*metabolism, Hordeum/enzymology, Bacterial, Gene Expression Regulation, Chlamydomonas reinhardtii/enzymology, Escherichia coli/*metabolism, Protein Subunits/metabolism, Recombinant Proteins/biosynthesis/genetics/metabolism, Chelatase, Chlorophyll biosynthesis, Magnesium, Oxidative stress, Protoporphyrin
in
Protein Expression and Purification
volume
101
pages
61 - 67
publisher
Academic Press
external identifiers
  • scopus:84903277435
ISSN
1046-5928
DOI
10.1016/j.pep.2014.06.004
language
English
LU publication?
no
id
877e0faf-e6ae-4365-baf2-c25587f6cddc (old id 8001728)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/24931499
date added to LUP
2015-09-30 09:59:25
date last changed
2017-07-02 03:09:48
@article{877e0faf-e6ae-4365-baf2-c25587f6cddc,
  abstract     = {The approximately 150kDa ChlH subunit of magnesium chelatase from Oryza sativa, Hordeum vulgare and Chlamydomonas reinhardtii have been heterologously expressed in Escherichiacoli. The active soluble protein is found as both a multimeric and a monomeric form. The multimeric ChlH appears to be oxidatively damaged but monomer production is favoured in growth conditions that are known to cause an oxidative stress response in E.coli. Inducing an oxidative stress response may be of general utility to improve the quality of proteins expressed in E. coli. The similar responses of ChlH's from the three different species suggest that oligomerization of oxidatively damaged ChlH may have a functional role in the chloroplast, possibly as a signal of oxidative stress or damage.},
  author       = {Muller, A. H. and Sawicki, A. and Zhou, S. and Tabrizi, S. T. and Luo, M. and Hansson, Mats and Willows, R. D.},
  issn         = {1046-5928},
  keyword      = {Protein Multimerization/*physiology,Oxidative Stress/*physiology,Oxidation-Reduction,Oryza sativa/enzymology,Lyases/*biosynthesis/genetics/*metabolism,Hordeum/enzymology,Bacterial,Gene Expression Regulation,Chlamydomonas reinhardtii/enzymology,Escherichia coli/*metabolism,Protein Subunits/metabolism,Recombinant Proteins/biosynthesis/genetics/metabolism,Chelatase,Chlorophyll biosynthesis,Magnesium,Oxidative stress,Protoporphyrin},
  language     = {eng},
  pages        = {61--67},
  publisher    = {Academic Press},
  series       = {Protein Expression and Purification},
  title        = {Inducing the oxidative stress response in Escherichia coli improves the quality of a recombinant protein: magnesium chelatase ChlH},
  url          = {http://dx.doi.org/10.1016/j.pep.2014.06.004},
  volume       = {101},
  year         = {2014},
}