Inducing the oxidative stress response in Escherichia coli improves the quality of a recombinant protein: magnesium chelatase ChlH
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8001728
- author
- Muller, A. H. ; Sawicki, A. ; Zhou, S. ; Tabrizi, S. T. ; Luo, M. ; Hansson, Mats LU and Willows, R. D.
- publishing date
- 2014
- type
- 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
- pmid:24931499
- 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
- 2016-04-01 10:18:12
- date last changed
- 2022-02-02 08:31:21
@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}},
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}},
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}},
doi = {{10.1016/j.pep.2014.06.004}},
volume = {{101}},
year = {{2014}},
}