scholarly journals Three-dimensional localization of the NH2- and carboxyl-terminal domain of ribosomal protein S1 on the surface of the 30 S subunit from Escherichia coli.

1990 ◽  
Vol 265 (19) ◽  
pp. 11338-11344
Author(s):  
J Walleczek ◽  
R Albrecht-Ehrlich ◽  
G Stöffler ◽  
M Stöffler-Meilicke
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Three Dimensional ◽  
Terminal Domain ◽  
Ribosomal Protein S1 ◽  
Carboxyl Terminal Domain ◽  
Carboxyl Terminal

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.

scholarly journals Direct Interaction of the N-Terminal Domain of Ribosomal Protein S1 with Protein S2 in Escherichia coli

PLoS ONE ◽  
2012 ◽  
Vol 7 (3) ◽  
pp. e32702 ◽  
Author(s):  
Konstantin Byrgazov ◽  
Salim Manoharadas ◽  
Anna C. Kaberdina ◽  
Oliver Vesper ◽  
Isabella Moll
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Protein ◽  
Direct Interaction ◽  
Terminal Domain ◽  
Ribosomal Protein S1
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