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 journalArticlepeer-review

5 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 languageEnglish
Pages (from-to)61-67
Number of pages7
JournalProtein Expression and Purification
Volume101
DOIs
Publication statusPublished - 2014

Keywords

  • oxidative stress
  • protoporphyrin
  • chlorophyll biosynthesis
  • chelatase
  • magnesium

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