PMID: 9537397Apr 16, 1998Paper

The active-site cysteines of the periplasmic thioredoxin-like protein CcmG of Escherichia coli are important but not essential for cytochrome c maturation in vivo

Journal of Bacteriology
Renata A FabianekLinda Thöny-Meyer

Abstract

A new member of the family of periplasmic protein thiol:disulfide oxidoreductases, CcmG (also called DsbE), was characterized with regard to its role in cytochrome c maturation in Escherichia coli. The CcmG protein was shown to be membrane bound, facing the periplasm with its C-terminal, hydrophilic domain. A chromosomal, nonpolar in-frame deletion in ccmG resulted in the complete absence of all c-type cytochromes. Replacement of either one or both of the two cysteine residues of the predicted active site in CcmG (WCPTC) led to low but detectable levels of Bradyrhizobium japonicum holocytochrome c550 expressed in E. coli. This defect, but not that of the ccmG null mutant, could be complemented by adding low-molecular-weight thiol compounds to growing cells, which is in agreement with a reducing function for CcmG.

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Citations

Feb 10, 2010·Photosynthesis Research·Hidehiro SakuraiKazuhito Inoue
Oct 3, 2012·Antioxidants & Redox Signaling·Seung-Hyun Cho, Jean-Francois Collet
Nov 22, 2000·The Journal of Biological Chemistry·R KruppD Missiakas
Mar 13, 1999·The Journal of Biological Chemistry·P H BessetteG Georgiou
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May 11, 2015·FEBS Letters·Isabelle S ArtsJean-François Collet
Dec 9, 2015·Journal of Bacteriology·Melissa E Reardon-Robinson, Hung Ton-That
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May 26, 1999·Proceedings of the National Academy of Sciences of the United States of America·H SchulzL Thöny-Meyer
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Jun 1, 2001·The Journal of Biological Chemistry·Q Ren, L Thony-Meyer
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May 15, 2010·The Journal of Biological Chemistry·Alan D GoddardStuart J Ferguson
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