scholarly journals The interplay between the disulfide bond formation pathway and cytochrome c maturation in Escherichia coli

FEBS Letters ◽  
2012 ◽  
Vol 586 (12) ◽  
pp. 1702-1707 ◽  
Author(s):  
Despoina A.I. Mavridou ◽  
Stuart J. Ferguson ◽  
Julie M. Stevens
Keyword(s):  
Escherichia Coli ◽  
Cytochrome C ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Cytochrome C Maturation ◽  
Formation Pathway

scholarly journals The Disulfide Bond Formation Pathway Is Essential for Anaerobic Growth of Escherichia coli

2017 ◽  
Vol 199 (16) ◽  
Author(s):  
Brian M. Meehan ◽  
Cristina Landeta ◽  
Dana Boyd ◽  
Jonathan Beckwith
Keyword(s):  
Escherichia Coli ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Anaerobic Growth ◽  
Strictly Anaerobic ◽  
Disulfide Bond Formation ◽  
Anaerobic Conditions ◽  
Content Type ◽  
E Coli ◽  
Laboratory Conditions

ABSTRACT Disulfide bonds are critical to the stability and function of many bacterial proteins. In the periplasm of Escherichia coli, intramolecular disulfide bond formation is catalyzed by the two-component disulfide bond forming (DSB) system. Inactivation of the DSB pathway has been shown to lead to a number of pleotropic effects, although cells remain viable under standard laboratory conditions. However, we show here that dsb strains of E. coli reversibly filament under aerobic conditions and fail to grow anaerobically unless a strong oxidant is provided in the growth medium. These findings demonstrate that the background disulfide bond formation necessary to maintain the viability of dsb strains is oxygen dependent. LptD, a key component of the lipopolysaccharide transport system, fails to fold properly in dsb strains exposed to anaerobic conditions, suggesting that these mutants may have defects in outer membrane assembly. We also show that anaerobic growth of dsb mutants can be restored by suppressor mutations in the disulfide bond isomerization system. Overall, our results underscore the importance of proper disulfide bond formation to pathways critical to E. coli viability under conditions where oxygen is limited. IMPORTANCE While the disulfide bond formation (DSB) system of E. coli has been studied for decades and has been shown to play an important role in the proper folding of many proteins, including some associated with virulence, it was considered dispensable for growth under most laboratory conditions. This work represents the first attempt to study the effects of the DSB system under strictly anaerobic conditions, simulating the environment encountered by pathogenic E. coli strains in the human intestinal tract. By demonstrating that the DSB system is essential for growth under such conditions, this work suggests that compounds inhibiting Dsb enzymes might act not only as antivirulents but also as true antibiotics.

scholarly journals Identification and Functional Analysis of an Immunoreactive DsbA-Like Thio-Disulfide Oxidoreductase of Ehrlichia spp.

2002 ◽  
Vol 70 (5) ◽  
pp. 2700-2703 ◽  
Author(s):  
Jere W. McBride ◽  
Lucy M. Ndip ◽  
Vsevolod L. Popov ◽  
David H. Walker
Keyword(s):  
Escherichia Coli ◽  
Functional Analysis ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Ehrlichia Canis ◽  
Disulfide Bond Formation ◽  
Ehrlichia Chaffeensis ◽  
Disulfide Oxidoreductase

ABSTRACT Novel homologous DsbA-like disulfide bond formation (Dsb) proteins of Ehrlichia chaffeensis and Ehrlichia canis were identified which restored DsbA activity in complemented Escherichia coli dsbA mutants. Recombinant Ehrlichia Dsb (eDsb) proteins were recognized by sera from E. canis-infected dogs but not from E. chaffeensis-infected patients. The eDsb proteins were observed primarily in the periplasm of E. chaffeensis and E. canis.

scholarly journals Trapping of conformations of the Escherichia coli F1 ATPase by disulfide bond formation

FEBS Letters ◽  
1998 ◽  
Vol 426 (1) ◽  
pp. 37-40 ◽  
Author(s):  
Robert Aggeler ◽  
Gerhard Grüber ◽  
Roderick A Capaldi
Keyword(s):  
Escherichia Coli ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
F1 Atpase
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