The role of Escherichia coli FhlA transcriptional activator in generation of proton motive force and F O F 1 ‐ATPase activity at pH  7.5

IUBMB Life ◽  
2021 ◽  
Author(s):  
Heghine Gevorgyan ◽  
Satenik Khalatyan ◽  
Anait Vassilian ◽  
Karen Trchounian
Keyword(s):  
Escherichia Coli ◽  
Atpase Activity ◽  
Transcriptional Activator ◽  
Proton Motive Force ◽  
Motive Force

scholarly journals The role of the proton motive force and electron flow in solute transport in Escherichia coli

1985 ◽  
Vol 153 (1) ◽  
pp. 161-165 ◽  
Author(s):  
Marieke G. L. ELFERINK ◽  
Klaas J. HELLINGWERF ◽  
Wil N. KONINGS
Keyword(s):  
Escherichia Coli ◽  
Solute Transport ◽  
Electron Flow ◽  
Proton Motive Force ◽  
Motive Force

scholarly journals Development of Escherichia coli virus T1. The role of the proton-motive force.

1980 ◽  
Vol 255 (2) ◽  
pp. 534-539
Author(s):  
E.F. Wagner ◽  
H. Ponta ◽  
M. Schweiger
Keyword(s):  
Escherichia Coli ◽  
Proton Motive Force ◽  
Motive Force

scholarly journals Interactions of haemoglobin with the Neisseria meningitidis receptor HpuAB: the role of TonB and an intact proton motive force

2002 ◽  
Vol 43 (2) ◽  
pp. 335-354 ◽  
Author(s):  
K. H. Rohde ◽  
A. F. Gillaspy ◽  
M. D. Hatfield ◽  
L. A. Lewis ◽  
D. W. Dyer
Keyword(s):  
Neisseria Meningitidis ◽  
Proton Motive Force ◽  
Motive Force

scholarly journals Changes in the proton-motive force in Escherichia coli in response to external oxidoreduction potential

1999 ◽  
Vol 262 (2) ◽  
pp. 595-599 ◽  
Author(s):  
Christophe Riondet ◽  
Remy Cachon ◽  
Yves Wache ◽  
, Gerard Alcaraz ◽  
Charles Divies
Keyword(s):  
Escherichia Coli ◽  
Proton Motive Force ◽  
Motive Force ◽  
Oxidoreduction Potential

scholarly journals In Vivo Synthesis of the Periplasmic Domain of TonB Inhibits Transport through the FecA and FhuA Iron Siderophore Transporters of Escherichia coli

2001 ◽  
Vol 183 (20) ◽  
pp. 5885-5895 ◽  
Author(s):  
S. Peter Howard ◽  
Christina Herrmann ◽  
Chad W. Stratilo ◽  
V. Braun
Keyword(s):  
Escherichia Coli ◽  
Cytoplasmic Membrane ◽  
Signal Sequence ◽  
Outer Membrane Proteins ◽  
Proton Motive Force ◽  
Motive Force ◽  
In Vivo Studies ◽  
Siderophore Transport

ABSTRACT The siderophore transport activities of the two outer membrane proteins FhuA and FecA of Escherichia coli require the proton motive force of the cytoplasmic membrane. The energy of the proton motive force is postulated to be transduced to the transport proteins by a protein complex that consists of the TonB, ExbB, and ExbD proteins. In the present study, TonB fragments lacking the cytoplasmic membrane anchor were exported to the periplasm by fusing them to the cleavable signal sequence of FecA. Overexpressed TonB(33-239), TonB(103-239), and TonB(122-239) fragments inhibited transport of ferrichrome by FhuA and of ferric citrate by FecA, transcriptional induction of the fecABCDE transport genes by FecA, infection by phage φ80, and killing of cells by colicin M via FhuA. Transport of ferrichrome by FhuAΔ5-160 was also inhibited by TonB(33-239), although FhuAΔ5-160 lacks the TonB box which is involved in TonB binding. The results show that TonB fragments as small as the last 118 amino acids of the protein interfere with the function of wild-type TonB, presumably by competing for binding sites at the transporters or by forming mixed dimers with TonB that are nonfunctional. In addition, the interactions that are inhibited by the TonB fragments must include more than the TonB box, since transport through corkless FhuA was also inhibited. Since the periplasmic TonB fragments cannot assume an energized conformation, these in vivo studies also agree with previous cross-linking and in vitro results, suggesting that neither recognition nor binding to loaded siderophore receptors is the energy-requiring step in the TonB-receptor interactions.

Sign in / Sign up

Export Citation Format

Share Document