scholarly journals 2P206 The flagellar P-ring component protein FlgI of Escherichia coli : Analysis of its intramolecular disulfide bond and ring assembly

2005 ◽  
Vol 45 (supplement) ◽  
pp. S171
Author(s):  
Y. Hizukuri ◽  
T. Yakushi ◽  
I. Kawagishi ◽  
M. Homma
Keyword(s):  
Escherichia Coli ◽  
Disulfide Bond ◽  
Ring Assembly ◽  
Intramolecular Disulfide Bond ◽  
Component Protein

scholarly journals Role of the Intramolecular Disulfide Bond in FlgI, the Flagellar P-Ring Component of Escherichia coli

2006 ◽  
Vol 188 (12) ◽  
pp. 4190-4197 ◽  
Author(s):  
Yohei Hizukuri ◽  
Toshiharu Yakushi ◽  
Ikuro Kawagishi ◽  
Michio Homma
Keyword(s):  
Escherichia Coli ◽  
Disulfide Bond ◽  
Self Assembly ◽  
Bacterial Species ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Wild Type ◽  
Ring Assembly ◽  
Intramolecular Disulfide Bond

ABSTRACT The P ring of the bacterial flagellar motor consists of multiple copies of FlgI, a periplasmic protein. The intramolecular disulfide bond in FlgI has previously been reported to be essential for P-ring assembly in Escherichia coli, because the P ring was not assembled in a dsbB strain that was defective for disulfide bond formation in periplasmic proteins. We, however, found that the two Cys residues of FlgI are not conserved in other bacterial species. We then assessed the role of this intramolecular disulfide bond in FlgI. A Cys-eliminated FlgI derivative formed a P ring that complemented the flagellation defect of our ΔflgI strain when it was overproduced, suggesting that disulfide bond formation in FlgI is not absolutely required for P-ring assembly. The levels of the mature forms of the FlgI derivatives were significantly lower than that of wild-type FlgI, although the precursor protein levels were unchanged. Moreover, the FlgI derivatives were more susceptible to degradation than wild-type FlgI. Overproduction of FlgI suppressed the motility defect of ΔdsbB cells. Additionally, the low level of FlgI observed in the ΔdsbB strain increased in the presence of l-cystine, an oxidative agent. We propose that intramolecular disulfide bond formation facilitates the rapid folding of the FlgI monomer to protect against degradation in the periplasmic space, thereby allowing its efficient self-assembly into the P ring.

scholarly journals Detection and function of an intramolecular disulfide bond in the pH-responsive CadC of Escherichia coli

2011 ◽  
Vol 11 (1) ◽  
pp. 74 ◽  
Author(s):  
Larissa Tetsch ◽  
Christiane Koller ◽  
Alexandra Dönhöfer ◽  
Kirsten Jung
Keyword(s):  
Escherichia Coli ◽  
Disulfide Bond ◽  
Ph Responsive ◽  
Intramolecular Disulfide Bond ◽  
And Function

scholarly journals Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme.

1991 ◽  
Vol 266 (10) ◽  
pp. 6456-6461 ◽  
Author(s):  
Y Taniyama ◽  
R Kuroki ◽  
F Omura ◽  
C Seko ◽  
M Kikuchi
Keyword(s):  
Disulfide Bond ◽  
Human Lysozyme ◽  
Intramolecular Disulfide Bond
Sign in / Sign up

Export Citation Format

Share Document