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

André H. Müller; Artur Sawicki; Shuaixiang Zhou; Shabnam Tarahi Tabrizi; Meizhong Luo; Mats Hansson; Robert D. Willows

doi:10.1016/j.pep.2014.06.004

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

André H. Müller, Artur Sawicki, Shuaixiang Zhou, Shabnam Tarahi Tabrizi, Meizhong Luo, Mats Hansson, Robert D. Willows^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

The ∼150 kDa ChlH subunit of magnesium chelatase from Oryza sativa, Hordeum vulgare and Chlamydomonas reinhardtii have been heterologously expressed in Escherichia coli. 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.

Original language	English
Pages (from-to)	61-67
Number of pages	7
Journal	Protein Expression and Purification
Volume	101
DOIs	https://doi.org/10.1016/j.pep.2014.06.004
Publication status	Published - Sept 2014

Keywords

oxidative stress
protoporphyrin
chlorophyll biosynthesis
chelatase
magnesium

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10.1016/j.pep.2014.06.004

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title = "Inducing the oxidative stress response in Escherichia coli improves the quality of a recombinant protein: Magnesium chelatase ChlH",

abstract = "The ∼150 kDa ChlH subunit of magnesium chelatase from Oryza sativa, Hordeum vulgare and Chlamydomonas reinhardtii have been heterologously expressed in Escherichia coli. 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.",

keywords = "oxidative stress, protoporphyrin, chlorophyll biosynthesis, chelatase, magnesium",

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T2 - Magnesium chelatase ChlH

AU - Müller, André H.

AU - Sawicki, Artur

AU - Zhou, Shuaixiang

AU - Tabrizi, Shabnam Tarahi

AU - Luo, Meizhong

AU - Hansson, Mats

AU - Willows, Robert D.

PY - 2014/9

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AB - The ∼150 kDa ChlH subunit of magnesium chelatase from Oryza sativa, Hordeum vulgare and Chlamydomonas reinhardtii have been heterologously expressed in Escherichia coli. 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.

KW - oxidative stress

KW - protoporphyrin

KW - chlorophyll biosynthesis

KW - chelatase

KW - magnesium

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SN - 1046-5928

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EP - 67

JO - Protein Expression and Purification

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ER -

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

Abstract

Keywords

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