scholarly journals The Regulatory C-Terminal Domain of Subunit   of FoF1 ATP Synthase Is Dispensable for Growth and Survival of Escherichia coli

2011 ◽  
Vol 193 (8) ◽  
pp. 2046-2052 ◽  
Author(s):  
N. Taniguchi ◽  
T. Suzuki ◽  
M. Berney ◽  
M. Yoshida ◽  
G. M. Cook
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Growth And Survival ◽  
Terminal Domain ◽  
Fof1 Atp Synthase

scholarly journals An alternative role of FoF1-ATP synthase in Escherichia coli: synthesis of thiamine triphosphate

2013 ◽  
Vol 3 (1) ◽  
Author(s):  
Tiziana Gigliobianco ◽  
Marjorie Gangolf ◽  
Bernard Lakaye ◽  
Bastien Pirson ◽  
Christoph von Ballmoos ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Thiamine Triphosphate ◽  
Fof1 Atp Synthase

scholarly journals Direct observation of steps in c-ring rotation of Escherichia coli FOF1-ATP synthase

2010 ◽  
Vol 1797 ◽  
pp. 34 ◽  
Author(s):  
Ryota Iino ◽  
Khek-Chian Tham ◽  
Kazuhito V. Tabata ◽  
Hiroshi Ueno ◽  
Hiroyuki Noji
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Direct Observation ◽  
Ring Rotation ◽  
Fof1 Atp Synthase

scholarly journals The regulatory subunit ε in Escherichia coli FOF1-ATP synthase

2018 ◽  
Vol 1859 (9) ◽  
pp. 775-788 ◽  
Author(s):  
Hendrik Sielaff ◽  
Thomas M. Duncan ◽  
Michael Börsch
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Regulatory Subunit ◽  
Fof1 Atp Synthase

scholarly journals Inhibition of F1-ATPase Rotational Catalysis by the Carboxyl-terminal Domain of the ϵ Subunit

2014 ◽  
Vol 289 (44) ◽  
pp. 30822-30831 ◽  
Author(s):  
Mayumi Nakanishi-Matsui ◽  
Mizuki Sekiya ◽  
Shio Yano ◽  
Masamitsu Futai
Keyword(s):  
Escherichia Coli ◽  
Atpase Activity ◽  
Atp Synthase ◽  
Single Molecule ◽  
Inhibitory Effect ◽  
Rotational Catalysis ◽  
Terminal Domain ◽  
Carboxyl Terminal Domain ◽  
Carboxyl Terminal ◽  
Loop 2

Escherichia coli ATP synthase (F0F1) couples catalysis and proton transport through subunit rotation. The ϵ subunit, an endogenous inhibitor, lowers F1-ATPase activity by decreasing the rotation speed and extending the duration of the inhibited state (Sekiya, M., Hosokawa, H., Nakanishi-Matsui, M., Al-Shawi, M. K., Nakamoto, R. K., and Futai, M. (2010) Single molecule behavior of inhibited and active states of Escherichia coli ATP synthase F1 rotation. J. Biol. Chem. 285, 42058–42067). In this study, we constructed a series of ϵ subunits truncated successively from the carboxyl-terminal domain (helix 1/loop 2/helix 2) and examined their effects on rotational catalysis (ATPase activity, average rotation rate, and duration of inhibited state). As expected, the ϵ subunit lacking helix 2 caused about ½-fold reduced inhibition, and that without loop 2/helix 2 or helix 1/loop 2/helix 2 showed a further reduced effect. Substitution of ϵSer108 in loop 2 and ϵTyr114 in helix 2, which possibly interact with the β and γ subunits, respectively, decreased the inhibitory effect. These results suggest that the carboxyl-terminal domain of the ϵ subunit plays a pivotal role in the inhibition of F1 rotation through interaction with other subunits.

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