scholarly journals A Potential Rotational Mechanism of the γ-Subunit of F1 - ATPase--Torque Generation through the Random Movement of an Asymmetric Rotor

2016 ◽  
Vol 110 (3) ◽  
pp. 312a
Author(s):  
Ya-chang Chou ◽  
Yi-Feng Hsiao
Genetics ◽  
1996 ◽  
Vol 144 (4) ◽  
pp. 1445-1454 ◽  
Author(s):  
Xin Jie Chen ◽  
G Desmond Clark-Walker

In a previous report, we found that mutations at the mitochondrial genome integrity locus, MGI1, can convert Kluyveromyces lactis into a petite-positive yeast. In this report, we describe the isolation of the MGI1 gene and show that it encodes the β-subunit of the mitochondrial F1-ATPase. The site of mutation in four independently isolated mgi1 alleles is at Arg435, which has changed to Gly in three cases and Ile in the fourth isolate. Disruption of MGI1 does not lead to the production of mitochondrial genome deletion mutants, indicating that an assembled F1 complex is needed for the “gain-of-function” phenotype found in mgi1 point mutants. The location of Arg435 in the β-subunit, as deduced from the three-dimensional structure of the bovine F1-ATPase, together with mutational sites in the previously identified mgi2 and mgi5 alleles, suggests that interaction of the β- and α- (MGI2) subunits with the γ-subunit (MGI5) is likely to be affected by the mutations.


2015 ◽  
Vol 112 (9) ◽  
pp. 2746-2751 ◽  
Author(s):  
Shayantani Mukherjee ◽  
Arieh Warshel

Unraveling the molecular nature of the conversion of chemical energy (ATP hydrolysis in the α/β-subunits) to mechanical energy and torque (rotation of the γ-subunit) in F1-ATPase is very challenging. A major part of the challenge involves understanding the rotary–chemical coupling by a nonphenomenological structure–energy description, while accounting for the observed torque generated on the γ-subunit and its change due to mutation of this unit. Here we extend our previous study that used a coarse-grained model of the F1-ATPase to generate a structure-based free energy landscape of the rotary–chemical process. Our quantitative analysis of the landscape reproduced the observed torque for the wild-type enzyme. In doing so, we found that there are several possibilities of torque generation from landscapes with various shapes and demonstrated that a downhill slope along the chemical coordinate could still result in negligible torque, due to ineffective coupling of the chemistry to the γ-subunit rotation. We then explored the relationship between the functionality and the underlying sequence through systematic examination of the effect of various parts of the γ-subunit on free energy surfaces of F1-ATPase. Furthermore, by constructing several types of γ-deletion systems and calculating the corresponding torque generation, we gained previously unknown insights into the molecular nature of the F1-ATPase rotary motor. Significantly, our results are in excellent agreement with recent experimental findings and indicate that the rotary–chemical coupling is primarily established through electrostatic effects, although specific contacts through γ-ionizable residue side chains are not essential for establishing the basic features of the coupling.


2017 ◽  
Vol 9 (2) ◽  
pp. 103-118 ◽  
Author(s):  
Hiroyuki Noji ◽  
Hiroshi Ueno ◽  
Duncan G. G. McMillan
Keyword(s):  

2012 ◽  
Vol 287 (46) ◽  
pp. 38695-38704 ◽  
Author(s):  
Ei-Ichiro Sunamura ◽  
Hiroki Konno ◽  
Mari Imashimizu ◽  
Mari Mochimaru ◽  
Toru Hisabori

2011 ◽  
Vol 101 (1) ◽  
pp. 188-195 ◽  
Author(s):  
Ayako Kohori ◽  
Ryohei Chiwata ◽  
Mohammad Delawar Hossain ◽  
Shou Furuike ◽  
Katsuyuki Shiroguchi ◽  
...  

2006 ◽  
Vol 90 (11) ◽  
pp. 4195-4203 ◽  
Author(s):  
Mohammad Delawar Hossain ◽  
Shou Furuike ◽  
Yasushi Maki ◽  
Kengo Adachi ◽  
M. Yusuf Ali ◽  
...  
Keyword(s):  

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